A Database of Drosophila Genes & Genomes

FB2012_01, released January 20th, 2012
 

Gene Dmel\Hsp70Ba

General Information
SymbolDmel\Hsp70BaSpeciesD. melanogaster
NameHeat-shock-protein-70BaAnnotation symbolCG31449
Feature typeprotein_coding_geneFlyBase IDFBgn0013277
Gene Model StatusCurrent Stock availability 3 publicly available
Also Known AsHsp70, hsp70B, dhsp70, hsp-70
Genomic Location
Chromosome (arm)3RRecombination map
Cytogenetic map87B12-87B12Sequence location3R:8,291,026..8,293,500 [-]

Genomic Maps

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modENCODE GBrowse
detailed view
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Automatically generated summary

See sections below for more information
The gene Heat-shock-protein-70Ba is referred to in FlyBase by the symbol Dmel\Hsp70Ba (CG31449, FBgn0013277). It is a protein_coding_gene from Drosophila melanogaster. An electronic pipeline based on InterPro domains suggests that it has the molecular function: ATP binding. There is experimental evidence that it is involved in the biological process: response to hypoxia; heat shock-mediated polytene chromosome puffing; response to heat. 5 alleles are reported. No phenotypic data is available. It has one annotated transcript and one annotated polypeptide. Protein features are: Heat shock protein 70; Heat shock protein 70, conserved site; Heat shock protein Hsp70. Summary of modENCODE Temporal Expression Profile: Temporal profile ranges from a peak of moderately high expression to a trough of extremely low expression. Peak expression observed at stages throughout the pupal period. Summary of FlyAtlas Anatomical Expression Data: No FlyAtlas data available because no Affy2 ProbeSet aligns to an exon of Hsp70Ba. Comments on Affy2 ProbeSet: No relevant information because no Affy2 ProbeSet aligns to an exon of Hsp70Ba. Gene sequence location is 3R:8291026..8293500.

hide Phenotypic Description from the Red Book (Lindsley & Zimm 1992)
Gene/Allele symbols may differ from current usage
Hsp70
The structural genes that code for the 70,000 dalton heat-shock protein (HSP70), the most abundant of the heat-shock proteins. HSP70 returns to preshock levels more rapidly than other heat-shock proteins following return to 25 (DiDomenico, Bugaisky, and Lindquist, 1982, Proc. Nat. Acad. Sci. USA 79: 6181-85). The protein becomes concentrated in nuclei during heat shock; disperses to cytoplasm during recovery; returns to nucleus upon further heat shock (Velazquez and Lindquist, 1984, Cell 36: 655-62). Appears not to be expressed in the testis in response to heat-shock stimulation (Bonner, Parks, Parker-Thornberg, Mortin, and Pelham, 1984, Cell 37: 979-91). Deletion of either the 87A7 or the 87C1 sequences does not eliminate the HSP70 heat-shock response; simultaneous deletion of both sequences does eliminate the HSP70 heat-shock response (Ish-Horowitz et al., 1979).
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Description
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What does this section not display?
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FB2011_10
FB2012_01
References
All updates Click here to see a list of all updates to this record from FB2010_08 and on.
hide Detailed Mapping Data
FlyBase Computed Cytological Location
Cytogenetic map
Evidence for location
87B12-87B12  
Limits computationally determined from genome sequence between P{PZ}svp07842 and P{lacW}Vha55j2E9  
Experimentally Determined Cytological Location
Cytogenetic map
Notes
References
87C1-87C1  
(determined by in situ hybridisation)  
87C-87C  
(determined by in situ hybridisation)  
87C-87C  
(determined by in situ hybridisation)  
87C1-87C1  
(determined by in situ hybridisation)  
87C1-87C1  
(determined by in situ hybridisation)  
87C1-87C1  
(determined by in situ hybridisation)  
Experimentally Determined Recombination Data
Location
Left of (cM)
Right of (cM)
Notes
hide Gene Model & Products
Please see the GBrowse view of Dmel\Hsp70Ba for information on other features
To submit a correction to a gene model please use the Contact FlyBase form
detailed view FBtr0082680 FBtr0082679 FBpp0082148 FBpp0082147 FBti0042823 FBti0101102 FBti0027568 FBti0039026 FBti0020956
Comments on Gene Model
hide Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Associated CDS (aa)
FBtr0082679
  2475
  641
Additional Transcript Data & Comments
Reported size (kB)
2.55 (northern blot)
Comments
External Data
Crossreferences
hide Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank protein
FBpp0082147  
70.2  
641  
5.49  
Additional Polypeptide Data & Comments
Reported size (kDa)
641 (aa); 70.27 (kD predicted)
Comments
External Data
Linkouts
Crossreferences
InterPro domains - A database of protein families, domains, and functional sites
hide Sequences Consistent with the Gene Model
DDBJ /
EMBL /
GenBank
DNA sequence
Protein sequence
Name
 
 
 
 
 
UniProtKB/Swiss-Prot
UniProtKB/TrEMBL
hide Mapped Features
Mapped Features have been reorganized, please see this article for details.
Additional mapped features and mutations can be found on GBrowse or related reports.
Type
Symbol & Location
Additional Notes
References
hide External Data
Linkouts
Crossreferences
hide Expression Data
hideTranscript Expression
Additional Descriptive Data
Marker for
Subcellular Localization
CV Term
Notes
hidePolypeptide Expression
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
Marker for
Subcellular Localization
CV Term
Notes
hide High-Throughput Expression Data
or
Untitled Document detailed view CG5608-RA Hsp70Ba-RA
See Gelbart and Emmert, 2010.10.13 for analysis details and data files for all genes.

modENCODE Temporal Expression Data for FBgn0013277


   Styles
Linear
Logarithmic
Heatmap
   Scales
max expr for FBgn0013277
Very low expression bin max
Moderate expression bin max
High expression bin max
Extremely high expression bin max

Summary of modENCODE Temporal Expression Profile: Temporal profile ranges from a peak of moderately high expression to a trough of extremely low expression. Peak expression observed at stages throughout the pupal period.
[download data (TSV)]

Guide to modENCODE expression level colors
 
No expression (0 - 0)
 
Extremely low expression (1 - 10)
 
Very low expression (11 - 100)
 
Low expression (101 - 400)
 
Moderate expression (401 - 1400)
 
Moderately high expression (1401 - 4000)
 
High expression (4001 - 10000)
 
Very high expression (10001 - 100000)
 
Extremely high expression (100001 - 2000000)

Linear, scaled to maximum FBgn0013277 expression level
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 
 312
embryo 10-12hr
 
 1315
embryo 12-14hr
 
 343
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 
 209
embryo 22-24hr
 
 127
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 
 136
white prepupae new
 
 168
white prepupae 12hr
 
 2423
white prepupae 24hr
 
 1267
pupae 2d postWPP
 
 1866
pupae 3d postWPP
 
 337
pupae 4d postWPP
 
 2386
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
Linear, scaled to Very low expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 (312)
embryo 10-12hr
 (1315)
embryo 12-14hr
 (343)
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 (209)
embryo 22-24hr
 (127)
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 (136)
white prepupae new
 (168)
white prepupae 12hr
 (2423)
white prepupae 24hr
 (1267)
pupae 2d postWPP
 (1866)
pupae 3d postWPP
 (337)
pupae 4d postWPP
 (2386)
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
Linear, scaled to Moderate expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 
 312
embryo 10-12hr
 
 1315
embryo 12-14hr
 
 343
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 
 209
embryo 22-24hr
 
 127
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 
 136
white prepupae new
 
 168
white prepupae 12hr
 (2423)
white prepupae 24hr
 
 1267
pupae 2d postWPP
 (1866)
pupae 3d postWPP
 
 337
pupae 4d postWPP
 (2386)
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
Linear, scaled to High expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 
 312
embryo 10-12hr
 
 1315
embryo 12-14hr
 
 343
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 
 209
embryo 22-24hr
 
 127
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 
 136
white prepupae new
 
 168
white prepupae 12hr
 
 2423
white prepupae 24hr
 
 1267
pupae 2d postWPP
 
 1866
pupae 3d postWPP
 
 337
pupae 4d postWPP
 
 2386
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
Linear, scaled to Extremely high expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 
 312
embryo 10-12hr
 
 1315
embryo 12-14hr
 
 343
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 
 209
embryo 22-24hr
 
 127
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 
 136
white prepupae new
 
 168
white prepupae 12hr
 
 2423
white prepupae 24hr
 
 1267
pupae 2d postWPP
 
 1866
pupae 3d postWPP
 
 337
pupae 4d postWPP
 
 2386
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
 Extremely high 
log, scaled to maximum FBgn0013277 expression level
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 
 312
embryo 10-12hr
 
 1315
embryo 12-14hr
 
 343
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 
 209
embryo 22-24hr
 
 127
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 
 136
white prepupae new
 
 168
white prepupae 12hr
 
 2423
white prepupae 24hr
 
 1267
pupae 2d postWPP
 
 1866
pupae 3d postWPP
 
 337
pupae 4d postWPP
 
 2386
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
log, scaled to Very low expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 (312)
embryo 10-12hr
 (1315)
embryo 12-14hr
 (343)
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 (209)
embryo 22-24hr
 127
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 136
white prepupae new
 (168)
white prepupae 12hr
 (2423)
white prepupae 24hr
 (1267)
pupae 2d postWPP
 (1866)
pupae 3d postWPP
 (337)
pupae 4d postWPP
 (2386)
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
log, scaled to Moderate expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 
 312
embryo 10-12hr
 
 1315
embryo 12-14hr
 
 343
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 
 209
embryo 22-24hr
 
 127
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 
 136
white prepupae new
 
 168
white prepupae 12hr
 2423
white prepupae 24hr
 
 1267
pupae 2d postWPP
 1866
pupae 3d postWPP
 
 337
pupae 4d postWPP
 2386
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
log, scaled to High expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 
 312
embryo 10-12hr
 
 1315
embryo 12-14hr
 
 343
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 
 209
embryo 22-24hr
 
 127
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 
 136
white prepupae new
 
 168
white prepupae 12hr
 
 2423
white prepupae 24hr
 
 1267
pupae 2d postWPP
 
 1866
pupae 3d postWPP
 
 337
pupae 4d postWPP
 
 2386
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
log, scaled to Extremely high expression
Developmental Stage   Expression Level
embryo 00-02hr
 
 31
embryo 02-04hr
 
 45
embryo 04-06hr
 
 58
embryo 06-08hr
 
 75
embryo 08-10hr
 
 312
embryo 10-12hr
 
 1315
embryo 12-14hr
 
 343
embryo 14-16hr
 
 54
embryo 16-18hr
 
 24
embryo 18-20hr
 
 84
embryo 20-22hr
 
 209
embryo 22-24hr
 
 127
larva L1
 
 23
larva L2
 
 22
larva L3 12hr old
 
 35
larva L3 puffstage 1-2
 
 10
larva L3 puffstage 3-6
 
 34
larva L3 puffstage 7-9
 
 136
white prepupae new
 
 168
white prepupae 12hr
 
 2423
white prepupae 24hr
 
 1267
pupae 2d postWPP
 
 1866
pupae 3d postWPP
 
 337
pupae 4d postWPP
 
 2386
adult male 01day
 
 78
adult male 05day
 
 57
adult male 30day
 
 14
adult female 01day
 
 40
adult female 05day
 
 23
adult female 30day
 
 28
Expression Level Scale
 None 
 Extremely low 
 Very low 
 Low 
 Moderate 
 Moderately high 
 High 
 Very high 
 Extremely high 
Heatmap
Developmental Stage   Expression Level
embryo 00-02hr
 
 
embryo 02-04hr
 
 
embryo 04-06hr
 
 
embryo 06-08hr
 
 
embryo 08-10hr
 
 
embryo 10-12hr
 
 
embryo 12-14hr
 
 
embryo 14-16hr
 
 
embryo 16-18hr
 
 
embryo 18-20hr
 
 
embryo 20-22hr
 
 
embryo 22-24hr
 
 
larva L1
 
 
larva L2
 
 
larva L3 12hr old
 
 
larva L3 puffstage 1-2
 
 
larva L3 puffstage 3-6
 
 
larva L3 puffstage 7-9
 
 
white prepupae new
 
 
white prepupae 12hr
 
 
white prepupae 24hr
 
 
pupae 2d postWPP
 
 
pupae 3d postWPP
 
 
pupae 4d postWPP
 
 
adult male 01day
 
 
adult male 05day
 
 
adult male 30day
 
 
adult female 01day
 
 
adult female 05day
 
 
adult female 30day
 
 

modENCODE Temporal Expression Data (Graveley et al., 2011)
FlyAtlas Anatomical Expression Data (Chintapalli et al., 2007)
hide Expression Clusters
A cluster of genes with similar mRNA expression dynamics across development.
hide External Data & Images
Linkouts
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
hide Alleles & Phenotypes
hide Summary of Allele Phenotypes
Lethality
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
hide Classical Alleles ( 4 )
For All Classical Alleles Show

Allele of Hsp70BaClassMutagenStocksKnown lesion
Hsp70Ba3042 Yes
Hsp70Bajockey0 Yes
Hsp70BaP.ArvZim0 Yes
Hsp70BaP.EC0 Yes
hide Alleles Carried on Transgenic Constructs ( 1 )
For All Alleles Carried on Transgenic Constructs Show

Allele of Hsp70BaClassMutagenStocksKnown lesion
Hsp70BaGLV210371 Yes
hide Aneuploid Aberrations
Disrupted in
Not disrupted in
hide Transgenic Constructs & Insertions
Transgenic Constructs
Type of construct
Name
Expression data
UAS construct
characterization construct
Insertions
Type of insertions
Name
Expression data
hide Gene Ontology: Function, Process & Cellular Component ( 5 unique terms )
hide Terms Based on Experimental Evidence ( 4 terms )
Molecular Function ( 0 terms)
Biological Process
CV term
References
inferred from mutant phenotype
inferred from expression pattern
inferred from mutant phenotype
Cellular Component
CV term
References
hide Terms Based on Predictions or Assertions ( 2 terms )
Molecular Function
CV term
References
inferred from electronic annotation with InterPro:IPR001023
Biological Process
CV term
References
non-traceable author statement
Cellular Component ( 0 terms)
hide Sequence Ontology: Class of Gene
hide Interactions & Pathways
hide Summary of Physical Interactions
Protein-protein
Interacting group
Assay
References
hide Summary of Genetic Interactions
Interacts with
Please look at the allele data for full details of the genetic interactions
Hsp70Ba allele
Gene
References
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Linkouts
BioGRID - A database of protein and genetic interactions
DroID - A comprehensive database of gene and protein interactions.
InterologFinder Protein-protein interactions (PPI) from both known and predicted PPI data sets.
hide Orthologs
Genome-wide drosophilid orthologs
Curated drosophilid orthologs
Linkouts
InParanoid A subset of ortholog calls from InParanoid.
  • Lottia gigantea (owl limpet)
  • Lottia gigantea (owl limpet)
OrthoDB (Arthropod subset) The hierarchical catalog of eukaryotic orthologs.
hide Stocks & Reagents
hide Stocks Listed in FlyBase ( 3 )
Bloomington
hide Genomic Clones ( 2 )
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
hide cDNA Clones ( 31 )
Please Note
This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
cDNA Clones, Fully Sequenced
BDGP DGC clones
Other clones
cDNA Clones, End Sequenced (ESTs)
BDGP DGC clones
Other clones
hide RNAi & Array Information
Linkouts
DRSC - Results from RNAi screens.
GenomeRNAi - GenomeRNAi – A database for cell-based and in vivo RNAi phenotypes and reagents
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Source for database identity of
Source for database merge of
Additional comments
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Flies with no copies of the Hsp70 genes (Hsp70Aa, Hsp70Ab, Hsp70Ba, Hsp70Bb, Hsp70Bbb and Hsp70Bc) are unable to survive a severe heat shock. These flies show a lengthened heat-shock response and developmental delay following a non-lethal heat shock.
Flies with no copies of the Hsp70 genes (Hsp70Aa, Hsp70Ab, Hsp70Ba, Hsp70Bb, Hsp70Bbb and Hsp70Bc) are viable and fertile.
Some Drosophila strains, including that sequenced in the Drosophila genome project have three, not two, tandemly repeated Hsp70 genes at 87C1 (in addition to a reverse orientation Hsp70 gene, Hsp70Ba, approximately 40kb upstream). The distal-most gene of the three tandem copies is Hsp70Bc. The inner two tandem copies are Hsp70Bb and Hsp70Bbb.
New annotation (CG31449) in release 3 of the genome annotation.
Area matching Drosophila heat shock gene at 87c,proximal end, Acc. No. K01294.
Natural variation in Hsp70 expression is analysed to study thermotolerance.
The rate and intensity of Hsp70Ba protein expression has been compared with tissue damage after heat shock.
Expression is rapidly induced in the testis after heat stress. Activation of Hsp70 in testes and heads necessitates the presence of a functional Hsf.
There is significant variation among 74 different 2nd chromosome lines and 70 different 3rd chromosome lines in response to heat shock, measured by mRNA accumulation.
d(GA.TC)n sequences can be found in the promoters of Hsp26 and the Hsp70 genes. In vitro assembly of mononucleosomes into short DNA fragments carrying d(GA.TC)n sequences of different lengths is very efficient. Nucleosome assembly is inhibited strongly when the d(GA.TC)n sequence forms a triple-stranded conformation. Triplex formation requires partial destabilisation of the nucleosome. Results indicate nucleosome assembly and triplex formation are competing processes.
Chromosome homologies of Muller's element D (J chromosome in the Paleartic species and XR chromosome arm in Nearctic species) and of element E (O chromosome in the Paleartic species and 2 chromosome in Nearctic species) have been confirmed by single copy probes in the species of the obscura group and in D.melanogaster.
Sodium salicylate induces activation of Hsf binding activity in salivary gland cells and Schneider SL2 tissue cells. Puffing of heat shock gene loci occurs in salivary glands but Hsp70 transcription is not induced suggesting puffing and transcription are separable events.
The in vitro binding of Hsf protein to the promoter region of a number of heat shock genes has been analysed.
UV cross linking technique has been used to study the in vivo distribution of Trl protein on Hsp70 and Hsp26. Prior to heat shock Trl protein is associated with the promoter regions of the uninduced Hsp70 and Hsp26 genes. Upon heat shock induction Trl protein is recruited to their transcription units with its distribution coincident with that of RNA polymerase II.
The molecular architecture of the Hsp70Ba promoter has been analysed by genomic footprinting.
RNA levels do not increase with age, so the observed increase in protein levels is due to post-transcriptional regulation. Aging-specific expression may be a result of oxidative damage.
Synthesis of heat shock proteins is inhibited by both short-chain fatty acids and their corresponding alcohols, compounds which have no observable effect on histone acetylation.
Gene contains an RNA polymerase II complex which pauses after synthesis of a short transcript. In vivo ultraviolet crosslinking techniques demonstrate phosphorylation of the carboxy terminal domain (CTD) of the large subunit of RNA polymerase II could either regulate the transition of polymerase from a paused to an elongated complex or be a consequence of the transition from paused to elongated.
Chromosome staining reveals that Trl and heat shock transcription factors (HSF) colocalises at Hsp70Ba.
The 87A7 Hsp70B region is bordered on the proximal and distal sides by two special chromatin structures, scs and scs'. An enhancer blocking assay based on the w gene demonstrates that the two nuclease hypersensitive regions that define part of the scs chromatin structure are essential for the blocking activity. The DNA sequence spanning the nuclease resistant core located between the two hypersensitive regions is dispensable.
The transcription of heat shock proteins, except Hsp83, is independent of the p200 subunit of initiation factor eIF-4F, eIF-4G.
RNA polymerase distribution on uninduced Hsp70 genes has been compared with the distribution of RNA polymerase on DRB (5,6,-Dichloro-1-β-D-ribofuranosylbenzimidazole)-inhibited induced Hsp70 genes.
Hsp70 proteins are of prime importance to heat tolerance.
Members of the hsc70 gene family (heat shock cognate genes) that reside within the same intracellular compartment in different organisms share greater amino acid identity than hsc70 proteins from the same organism but different organelles. This pattern of conservation indicates specialisation of hsc70 function.
Identified in 2D gels of CMW W2 wing imaginal disc cell proteins.
Nascent chain nuclear run-on assays in KC161 cells reveal different responses to heat shock for different genes. Transcription of His1 is severely inhibited under mild heat shocks, of Act5C decreases proportionally with increasing temperature while that of the core histone genes or the heat shock cognates is repressed only under extreme heat shock. In unshocked cells Hsp83 is moderately transcribed while transcription from the other heat shock genes is undetectable. Engaged but paused RNA molecules are found at the various Hsp70 and Hsp26 genes but not at the other heat shock genes. Increased transcription of the heat shock genes is observed within 1-2 mins of heat shock and maximal rates were reached within 2-5 minutes. Rates of transcription vary over a 20-fold range. Hsrω is transcribed at a very high rate under non-heat shock conditions, and its response to elevated temperatures is different from that of the protein coding heat shock genes.
Hsp70 promoter driven expression in heat induced and non-heat induced conditions is more efficient in D.melanogaster embryos than in L.cuprina embryos.
The interaction of Top1 and Top2 gene products with transcriptionally active and inactive Hsp70B has been compared. Topoisomerase I binding sites are found in the transcribed portions of the Hsp70B gene, and only when Hsp70B is transcriptionally active. Topoisomerase II binding to Hsp70B sequences occurs on both transcriptionally active and inactive chromatin. An unusual type of topoisomerase II binding site is associated with the 5' ends of inactive Hsp70 gene, suggesting that this enzyme may be associated with repression of gene transcription.
The effect of aging on the expression of the "Hsp70" genes (Hsp70Aa, Hsp70Ab, Hsp70Ba, Hsp70Bb and Hsp70Bc) has been studied.
Translation of Hsp70 mRNAs and to a lesser extent the mRNAs for the small heat shock proteins is almost independent of eIF-4E.
Induction of heat shock protein after metal ion exposure is studied.
Sequences located 5' to Sgs7, Sgs8, Sgs3, the Hsp70 genes at 87A and 87C and the copia coding region are similar to the sequence at -405 from Sgs4.
initiates the heat-shock response. A restricted subset of genes, the Hsp genes, is activated and the majority of transcription and translation is shut down. However, mitochondrial- and histone-gene activities persist (Spradling, Pardue and Penman, 1977). This response follows a pulse of 36oC to 40oC; treatments above 40oC inhibit all activity and lead to death; treatments of 30oC-35oC induce heat-shock-protein synthesis without repressing normal protein synthesis (Tissieres, Mitchell and Tracy, 1974). Similar response inducible by other stressful treatments. The response may be elicited at all stages of the life cycle and in cultured cells. Stage specific phenocopies result from heat shocking early stages of Drosophila development (Mitchell and Petersen, 1982). In polytene cells existing puffs regress and a novel group quickly appears at 33B, 63C, 64F, 67B, 70A, 87A, 87C, 93D, 95D (Ashburner, 1970; Tissieres, Mitchell and Tracy, 1974). Activation of transcription of Hsp genes apparently involves the sequential binding of two or more protein factors in vicinity of TATA box (Wu, 1984). Binding sites for these proteins are multiple short upstream sequence elements called HSEs or heat shock consensus elements (Pelham, 1982; Xiao and Lis, 1988). Polymerase II dissociates from most chromosome regions and accumulates at the new puff sites (Bonner and Kerby, 1982). 3H-uridine incorporation ceases at its usual positions and commences at new puff sites. Preexisting polysomes disaggregate and within a few minutes a new population of polysomes appears containing newly transcribed mRNA; this RNA hybridizes to some of the heat-shock puffs. The effects of heat shock may be abrogated to some degree by pretreatment with a pulse of a slightly lower temperature (Mitchell, Moller, Petersen and Lipps-Sarmiento, 1979; Peterson and Mitchell, 1981). For reviews of the heat-shock response see Ashburner and Bonner (1978).
 
One of five structural genes (in two clusters, Hsp70A and Hsp70B) that code for the 70,000 dalton heat-shock protein (HSP70), the most abundant of the heat-shock proteins. Hsp70B usually includes three HSP70 encoding genes (Hsp70Ba (proximal), Hsp70Bb (middle), Hsp70Bc (distal)) (Holmgren, Livak, Morimoto, Freund, and Meselson, 1979) with slightly different restriction maps (Artavanis-Tsakonas et al., 1978). HSP70 returns to preshock levels more rapidly than other heat-shock proteins following return to 25oC (DiDomenico, Bugaisky and Lindquist, 1982). The protein becomes concentrated in nuclei during heat shock; disperses to cytoplasm during recovery; returns to nucleus upon further heat shock (Velazquez and Lindquist, 1984). Appears not to be expressed in the testis in response to heat-shock stimulation (Bonner, Parks, Parker-Thornberg, Mortin and Pelham, 1984). Deletion of either Hsp70A or Hsp70B does not eliminate the HSP70 heat-shock response; simultaneous deletion of both does (Ish-Horowicz et al., 1979).
 
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hide Synonyms & Secondary IDs ( 22 )
Reported As
Symbol Synonym
Hsp70
(Baker and Russell, 2009, Auluck et al., 2005, Scholz et al., 2005, Ahmed and Duncan, 2004, Jennings et al., 2004, Zhai et al., 2004, Gruntenko et al., 2003, Morrow et al., 2004, Temme et al., 2004, Marsh and Thompson, 2004, Sathyanarayanan et al., 2004, Jin et al., 2004, Canamasas et al., 2003, Norry and Loeschcke, 2003, Rutherford, 2003, Silbermann and Tatar, 2000, Sejerkilde et al., 2003, Krebs, 1999, Lakhotia et al., 2002, Auluck and Bonini, 2003, Caletka and Fry, 2003, Shaw et al., 2002, Auluck et al., 2002, Rajendra et al., 2001, Sorensen and Loeschcke, 2001, Bulgheresi et al., 2001, Mok et al., 2001, Zatsepina et al., 2001, Kelty and Lee, 2001, de Carcer et al., 2001, Ekengren and Hultmark, 2001, Wu et al., 2001, Krebs et al., 2001, Andrulis et al., 2000, Gunawardena and Rykowski, 2000, White et al., 1999, Feder, 1999, Elefant and Palter, 1999, Jazwinski, 1998, Dahlgaard et al., 1998, Wang and Lindquist, 1998, Cossins, 1998, Gu, 1998, Ashburner et al., 1998, Krebs et al., 1998, Michaud et al., 1997, Krebs and Feder, 1997, Krebs and Feder, 1997, Krebs and Feder, 1997, Espinas et al., 1996, Winegarden et al., 1996, Kingston et al., 1996, Engel and Cornelius, 1995, Weber and Gilmour, 1995, Li and Duncan, 1995, O'Brien et al., 1995, Gehring and Wehner, 1995, Lis and Wu, 1994, Fernandes et al., 1994, Parsell et al., 1993, Evgen'ev and Denisenko, 1990, Papaconstantinou et al., 2006, Behr et al., 2006, Shilova et al., 2006, Fernandez-Funez et al., 2007, Sengupta, 2006, Tenney et al., 2006, Smith et al., 2008, Ahrens et al., 2007, Zobeck et al., 2010, Hanyu-Nakamura et al., 2008, Eissenberg et al., 2007, Morettini et al., 2011, Bonini, 2002, Mito et al., 2007, Huen and Chan, 2005, Brandt and Corces, 2008, Newman et al., 2005, Yao et al., 2007, Ni et al., 2008, Iijima-Ando et al., 2005, Cai et al., 2008, Gilchrist et al., 2008, Lerman and Feder, 1999, Chopra et al., 2009, Kalosaka et al., 2006, Nielsen et al., 2005, Overgaard et al., 2005, Kristensen et al., 2003, Liévens et al., 2008, Cobreros et al., 2008, Piacentini et al., 2009, Tian et al., 2010, Bartkowiak et al., 2010, Hrizo and Palladino, 2010, Kwon et al., 2010, Zobeck et al., 2010, Jensen et al., 2010, Krebs and Holbrook, 2001, Neal et al., 2006, Fujikake et al., 2008, Gupta et al., 2005, Duncan, 2005, McLear et al., 2008, Rezaval et al., 2007)
hsp70
(Adelman et al., 2005, Wang et al., 2004, Matsumoto and Hirose, 2004, Landis et al., 2004, Smith et al., 2004, Ni et al., 2004, Saunders et al., 2005, Venkaiah et al., 2004, Lehmann, 2004, Viswanathan et al., 2003, Helfand and Rogina, 2003, Goodman et al., 2004, Tatar and Yin, 2001, Saunders et al., 2003, Kellum, 2003, Shaw and Franken, 2003, Feder, 2003, Geyer et al., 2000, Mahowald, 2001, Wimmer, 2003, Gilmour, 2003.4.18, Aigaki et al., 2002, Tulin and Spradling, 2003, Andrulis et al., 2002, Gong and Golic, 2003, Goodman et al., 2003, Kazantsev et al., 2002, Lakhotia and Prasanth, 2002, Herold et al., 2001, Gatfield et al., 2001, Biggin, 2001, Crevel et al., 2001, Christoffels et al., 2000, Badenhorst and Wu, 2001, Leach et al., 2000, Farkas et al., 2000, Yueh and Schneider, 2000, Lakhotia et al., 1999, Tatar, 1999, Feder, 1999, Hirayoshi and Lis, 1999, Bonini, 1999, Wu et al., 1998, Lis, 1998, Karunanithi et al., 1999, Mannervik, 1999, Sah et al., 1999, King and Tower, 1999, Katsani et al., 1999, Carr and Biggin, 1999, Zhao and Eggleston, 1999, Wilkins and Lis, 1999, Agianian et al., 1999, Nevo, 1998, Gdula et al., 1998, Yiangou et al., 1997, Wu and Fallon, 1997, Wilkins and Lis, 1998, Vernick and McCutchan, 1998, John and Workman, 1998, Curtsinger et al., 1997, Liang and Biggin, 1998, Gregory and Horz, 1998, Martinez-Balbas et al., 1998, Greenblatt, 1997, Wilkins and Lis, 1997, Finch and Tanzi, 1997, Otsuka et al., 1997, Tower, 1996, Shopland and Lis, 1996, Sandaltzopoulos et al., 1994, Segarra et al., 1996, O'Brien et al., 1994, Fernandes et al., 1995, Elefant and Palter, 1995, Wheeler et al., 1995, Rasmussen and Lis, 1995, Granok et al., 1995, Munks and Turner, 1994, Parsell and Lindquist, 1993, Zapata et al., 1994, Krumm et al., 1993, Fuller, 1993, Soeller et al., 1993, Lakhotia et al., 1993, Giardina and Lis, 1993, O'Brien and Lis, 1993, Molto et al., 1993, Heikkila, 1993, Papaceit and Juan, 1993, Vazquez et al., 1993, Morse, 1992, Fleming et al., 1992, Atkinson and O'Brochta, 1992, Pauli et al., 1992, Read and Manley, 1992, Becker et al., 1991, Niedzwiecki et al., 1991, Zapata et al., 1991, Bendena et al., 1991, Sorger, 1991, Spencer and Groudine, 1990, Helms and Rottman, 1990, Perkins et al., 1990, Karlin et al., 1990, Ornelles and Penman, 1990, Elgin, 1990, Menke and Petersen, 1989, Petersen and Lindquist, 1989, Petersen and Lindquist, 1988, Buszczak and Spradling, 2006, Kim and Lis, 2005, Graves and Tamkun, 2006, Halfon and Arnosti, 2007, Yao et al., 2006, Boeke et al., 2011, Wu et al., 2005, Piel et al., 2008, Schwartz et al., 2003, Boehm et al., 2003, Ullah et al., 2007, Ivaldi et al., 2007, Smith et al., 2008, Behm-Ansmant et al., 2007, Kurshakova et al., 2007, Hsu et al., 2008, Bettencourt and Feder, 2000, Zhao et al., 2005, Li et al., 2001, Poels et al., 2004, Yang and Tower, 2009, Tombácz et al., 2009, Chan et al., 2011, Vazquez-Pianzola et al., 2007, Kopytova et al., 2010, Kotova et al., 2010, Juge et al., 2010, Weisbrot et al., 2003, Ardehali et al., 2011, Ghosh et al., 2011)
Hsp70(87C)
Name Synonym
heat shock 70
Heat-shock-protein-70Ba
 
Secondary FlyBase IDs
  • FBgn0001232
  • FBgn0051449
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hide Recent research papers ( 18 )
Ardehali et al., 2011, EMBO J. 30(14): 2817--2828
Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with role in transcription. [FBrf0214333]
Boeke et al., 2011, PLoS ONE 6(6): e20761
The RNA Helicase Rm62 Cooperates with SU(VAR)3-9 to Re-Silence Active Transcription in Drosophila melanogaster. [FBrf0213941]
Casper et al., 2011, Development 138(16): 3357--3366
no child left behind encodes a novel chromatin factor required for germline stem cell maintenance in males but not females. [FBrf0214565]
Chan et al., 2011, Hum. Mol. Genet. 20(9): 1738--1750
Expanded polyglutamine domain possesses nuclear export activity which modulates subcellular localization and toxicity of polyQ disease protein via exportin-1. [FBrf0214367]
Ghosh et al., 2011, Mol. Cell. Biol. 31(20): 4232--4243
Negative Elongation Factor Accelerates the Rate at Which Heat Shock Genes Are Shut off by Facilitating Dissociation of Heat Shock Factor. [FBrf0215827]
Morettini et al., 2011, Nucleic Acids Res. 39(8): 3103--3115
The chromodomains of CHD1 are critical for enzymatic activity but less important for chromatin localization. [FBrf0213515]
Takahashi et al., 2011, PLoS ONE 6(4): e17295
Environmental Stress-Dependent Effects of Deletions Encompassing Hsp70Ba on Canalization and Quantitative Trait Asymmetry in Drosophila melanogaster. [FBrf0213649]
Bartkowiak et al., 2010, Genes Dev. 24(20): 2303--2316
CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1. [FBrf0212082]
Hrizo and Palladino, 2010, Neurobiol. Disease 40(3): 676--683
Hsp70- and Hsp90-mediated proteasomal degradation underlies TPI(sugarkill) pathogenesis in Drosophila. [FBrf0212050]
Jensen et al., 2010, J. Exp. Zoolog. Part A Comp. Exp. Biol. 313(1): 35--44
Adult heat tolerance variation in Drosophila melanogaster is not related to Hsp70 expression. [FBrf0209599]
Juge et al., 2010, PLoS Genet. 6(9): e1001124
The SR protein B52/SRp55 is required for DNA topoisomerase I recruitment to chromatin, mRNA release and transcription shutdown. [FBrf0211891]
Kopytova et al., 2010, Genes Dev. 24(1): 86--96
Multifunctional factor ENY2 is associated with the THO complex and promotes its recruitment onto nascent mRNA. [FBrf0209575]
Kotova et al., 2010, Proc. Natl. Acad. Sci. U.S.A. 107(14): 6406--6411
Uncoupling of the transactivation and transrepression functions of PARP1 protein. [FBrf0210529]
Kwon et al., 2010, Genes Dev. 24(19): 2133--2145
Heterochromatin protein 1 (HP1) connects the FACT histone chaperone complex to the phosphorylated CTD of RNA polymerase II. [FBrf0212000]
Papaconstantinou et al., 2010, PLoS ONE 5(11): e14049
Menin Links the Stress Response to Genome Stability in Drosophila melanogaster. [FBrf0212463]
Takahashi et al., 2010, BMC Evol. Biol. 10: 284
Effects of small Hsp genes on developmental stability and microenvironmental canalization. [FBrf0211941]
Tian et al., 2010, PLoS ONE 5(5): e10669
Phylogeny Disambiguates the Evolution of Heat-Shock cis-Regulatory Elements in Drosophila. [FBrf0210820]
Zobeck et al., 2010, Mol. Cell 40(6): 965--975
Recruitment timing and dynamics of transcription factors at the hsp70 Loci in living cells. [FBrf0212598]
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