A Database of Drosophila Genes & Genomes

FB2012_01, released January 20th, 2012
 

Gene Dmel\His4

General Information
SymbolDmel\His4SpeciesD. melanogaster
NameHistone H4Annotation symbol
Feature typeprotein_coding_geneFlyBase IDFBgn0001200
Gene Model StatusNot Applicable Stock availability 2 publicly available
Also Known AsH4, H4Ac16, HisC
Genomic Location
Chromosome (arm)Recombination map2-55
Cytogenetic map39D3-39E1Sequence location
hide Summary Information
Automatically generated summary

See sections below for more information
The gene Histone H4 is referred to in FlyBase by the symbol Dmel\His4 (FBgn0001200). This gene record represents a gene family, individual members of the family are: CG31611, CG33869, CG33871, CG33873, CG33875, CG33877, CG33879, CG33881, CG33883, CG33885, CG33887, CG33889, CG33891, CG33893, CG33895, CG33897, CG33899, CG33901, CG33903, CG33905, CG33907, CG33909. It is reported to have molecular function: DNA binding. There is experimental evidence that it is involved in the biological process: female meiosis chromosome segregation. 3 alleles are reported. No phenotypic data is available. It has no annotated transcripts. Protein features are: Histone H4; Histone H4, conserved site; Histone core; Histone-fold. Gene has not been localized to the genome sequence.

External Summaries

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Description
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What does this section not display?
This section does not currently display links that were removed or gene model changes.
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atom feed
FB2011_10
FB2012_01
References
Vatolina et al., 2011, Genetika, Moscow 47(5): 597--609
Vatolina et al., 2011, Russ. J. Genet. 47(5): 521--532
Guertin and Lis, 2010, PLoS Genet. 6(9):
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
39D3-39E1  
Left limit from in situ hybridisation (FBrf0029738) Right limit from molecular mapping relative to His2A (FBrf0044950)  
Experimentally Determined Cytological Location
Cytogenetic map
Notes
References
39D-39E  
(determined by in situ hybridisation)  
(Papaceit and Juan, 1993)
39D-39E  
(determined by in situ hybridisation)  
(Fitch et al., 1990)
39D3-39E2  
(determined by in situ hybridisation)  
(Pardue et al., 1977)
Experimentally Determined Recombination Data
Location
2-55
 
Left of (cM)
Right of (cM)
Notes
hide Gene Model & Products
Comments on Gene Model
hide Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Associated CDS (aa)
Additional Transcript Data & Comments
Reported size (kB)
Comments
External Data
Crossreferences
hide Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank protein
Additional Polypeptide Data & Comments
Reported size (kDa)
Comments
External Data
Linkouts
Crossreferences
InterPro domains - A database of protein families, domains, and functional sites
•
Histone H4 (IPR001951)
Histone core (IPR007125)
Histone-fold (IPR009072)
Histone H4, conserved site (IPR019809)
hide Sequences Consistent with the Gene Model
DDBJ /
EMBL /
GenBank
DNA sequence
Protein sequence
Name
BH840401
 
X14215
CAA32435
 
 
UniProtKB/Swiss-Prot
UniProtKB/TrEMBL
hide Mapped Features
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
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
fertilized egg stage  
female pronucleus  
• chromatin
(Loppin et al., 2001)
male pronucleus  
• chromatin
(Loppin et al., 2001)
embryonic stage 14 | male  
organism | anterior  
(Bhattacharya et al., 1999)
Comment:antibody specific to acylated protein
adult stage  
spermatid | late  
• chromatin
(Loppin et al., 2001)
spermatid | early  
• chromatin
(Loppin et al., 2001)
spermatozoon  
• chromatin
(Loppin et al., 2001)
Additional Descriptive Data
The pattern of binding of H4Ac16 along the male X chromosome is largely coincident with that of mle and msl-1.
(Loppin et al., 2001, Bone et al., 1994)
Marker for
Subcellular Localization
CV Term
chromosome
(Bone et al., 1994)
Notes
hide High-Throughput Expression Data
hide Expression Clusters
hide External Data & Images
Linkouts
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
•
hide Alleles & Phenotypes
hide Summary of Allele Phenotypes
Other Phenotypes
Allele
meiotic cell cycle defective | dominant
Phenotype manifest in
Allele
hide Classical Alleles ( 2 )
For All Classical Alleles Show

Allele of His4ClassMutagenStocksKnown lesion
His4KG002871 --
His4Scim1 Yes
hide Alleles Carried on Transgenic Constructs ( 1 )
For All Alleles Carried on Transgenic Constructs Show

Allele of His4ClassMutagenStocksKnown lesion
His4hs.T:Avic\GFP0 Yes
hide Aneuploid Aberrations
Disrupted in
(Moore et al., 1981)
Duplicated in
(Moore et al., 1981)
hide Transgenic Constructs & Insertions
Transgenic Constructs
Type of construct
Name
Expression data
Insertions
Type of insertions
Name
Expression data
miscellaneous insertions
P{SUPor-P}His4KG00287
NA
P{SUPor-P}His4Scim
NA
insertion of mobile activating element
P{GSV1}GSd206GSd206
NA
hide Gene Ontology: Function, Process & Cellular Component ( 6 unique terms )
hide Terms Based on Experimental Evidence ( 2 terms )
Molecular Function ( 0 terms)
Biological Process
CV term
Evidence
References
female meiosis chromosome segregation
inferred from mutant phenotype
(Dobie et al., 2001)
Cellular Component
CV term
Evidence
References
RCAF complex
inferred from direct assay
(Tyler et al., 1999)
hide Terms Based on Predictions or Assertions ( 4 terms )
Molecular Function
CV term
Evidence
References
DNA binding
inferred from electronic annotation with InterPro:IPR001951, InterPro:IPR007125, InterPro:IPR009072, InterPro:IPR019809
(FlyBase Curators et al., 2004-)
non-traceable author statement
(Swiss-Prot Project Members, 1986.7.21)
Biological Process
CV term
Evidence
References
chromatin assembly or disassembly
non-traceable author statement
(Swiss-Prot Project Members, 1986.7.21)
nucleosome assembly
inferred from electronic annotation with InterPro:IPR001951, InterPro:IPR019809
(FlyBase Curators et al., 2004-)
Cellular Component
CV term
Evidence
References
nucleosome
inferred from electronic annotation with InterPro:IPR001951, InterPro:IPR019809
(FlyBase Curators et al., 2004-)
non-traceable author statement
(Swiss-Prot Project Members, 1986.7.21)
traceable author statement
(Leach et al., 2000)
hide Sequence Ontology: Class of Gene
member_gene_array
 
nuclear_gene
 
protein_coding_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
His4 allele
Gene
References
hide External Data
Linkouts
hide Orthologs
Genome-wide drosophilid orthologs
Curated drosophilid orthologs
(Larsson et al., 2004)
(Larsson et al., 2004)
 
(Calvi et al., 2007)
 
 
 
(Larsson et al., 2004)
 
 
(Calvi et al., 2007)
 
 
 
 
 
 
(Larsson et al., 2004)
 
Linkouts
hide Stocks & Reagents
hide Stocks Listed in FlyBase ( 2 )
Bloomington
14797
y1; P{SUPor-P}His4Scim; ry506
14347
y1; P{SUPor-P}His4KG00287/SM6a; ry506
hide Genomic Clones ( 0 )
hide cDNA Clones ( 0 )
cDNA Clones, Fully Sequenced
BDGP DGC clones
Other clones
cDNA Clones, End Sequenced (ESTs)
BDGP DGC clones
Other clones
hide RNAi & Array Information
Linkouts
hide Antibody Information
monoclonal
(Egelhofer et al., 2011)
polyclonal
(Egelhofer et al., 2011)
hide Other Information
hide Discoverer
hide Etymology
hide Identification
hide Relationship to Other Genes
Source for database identity of
Source for database merge of
Encoded by
HIS-C
 
Component gene(s)
His4:CG31611
 
His4:CG33869
 
His4:CG33871
 
His4:CG33873
 
His4:CG33875
 
His4:CG33877
 
His4:CG33879
 
His4:CG33881
 
His4:CG33883
 
His4:CG33885
 
His4:CG33887
 
His4:CG33889
 
His4:CG33891
 
His4:CG33893
 
His4:CG33895
 
His4:CG33897
 
His4:CG33899
 
His4:CG33901
 
His4:CG33903
 
His4:CG33905
 
His4:CG33907
 
His4:CG33909
 
Additional comments
hide Other Comments
Transcriptional activation by ash1 coincides with methylation of lysines 4 and 9 of His3 and lysine 20 of His4 at the promoter of ash1 target genes.
(Beisel et al., 2002)
Disruption of pr-set7 reduces levels of His4 K20 methylation. His4 K20 methylation does not correlate with gene activity.
(Fang et al., 2002)
Lysine-20-methylated His4 is localized to chromatin-dense and transcriptionally silent regions. There is an inverse correlation in the number and intensity of bands containing methyl His4-K20 and acetyl His4-K16. Methylation of His4 lysine 20 maintains silent chromatin, in part, by precluding neighbouring acetylation on the His4 tail.
(Nishioka et al., 2002)
Mutations in Iswi affect both cell viability and gene expression during development.
(Deuring et al., 2000)
Replication-coupling assembly factor (RCAF) is a protein complex that facilitates the assembly of nucleosomes onto newly replicated DNA in vitro. RCAF is comprised of asf1, His3 and His4.
(Tyler et al., 1999)
In male germ cells, acetylated His4 appears to correlate with the general activity state of the chromosome rather than to an X-specific dosage compensation mechanism. Loss of mle has no detectable effect on expression or localisation of acetylated His4.
(Rastelli and Kuroda, 1998)
The majority of replication-dependent histone gene transcripts are not polyadenylated and in addition two types of polyadenylated transcripts can be detected. A small proportion of the histone mRNAs bear a short poly(A) tail which is added to the 3' terminus of a partially degraded stem-loop structure. Polyadenylation signals can be located downstream of the stem-loop structure that can be used to generate mRNAs with a poly(A) tail.
(Akhmanova et al., 1997)
The ATPase activity of Iswi is completely inhibited by each of the four histone tails (His2A, His2B, His3 and His4), results indicate a novel role for the flexible histone tails in chromatin remodeling by Iswi.
(Georgel et al., 1997)
Male-specific lethal (MSL) proteins accumulate in a subregion of male nuclei (the X chromosome) beginning at late blastoderm stage. X chromosomal binding of the MSLs is observed throughout embryonic and larval development in both diploid and polytene tissues. His4 colocalises with the MSLs in embryos.
(Franke et al., 1996)
HIS4-Ac16 is bound to the polytene X chromosome, as seen by antibody staining.
(Steinemann et al., 1996)
Immunostaining of embryonic and larval stages demonstrates that His4, msl-1 and msl-3 are associated with the male X chromosome as early as gastrulation, while mle binding is not detected until the late embryonic/late larval stages.
(Franke and Baker, 1995)
His4 is first detected on the X chromosome at stage 8 following msl-2 expression.
(Rastelli and Kuroda, 1995)
Expression pattern and localisation of mle, msl-1, msl-2 and His4 proteins are determined and results suggest that the protein associated with the X chromosome and are interdependent since early embryogenesis.
(Rastelli et al., 1995)
Lys5 and Lys12 are utilised during deposition-related His4 diacetylation.
(Sobel et al., 1995)
The gene products of mle, msl-1 bind to the male X chromosome in an identical pattern, and the binding sites of H4Ac16 acetylated form of the His4 product are largely coincident with the mle/msl-1 binding sites. This localisation of H4Ac16 protein is dependent on the dosage compensation regulatory pathway.
(Bone et al., 1994)
Both carnitine and butyrate compounds induce an accumulation of hyperacetylated H4 histones on chromatin.
(Fanti et al., 1994)
Antisera to H4Ac16 label the euchromatic X chromosome through mitosis, but neither the X heterochromatin nor autosomes.
(Lavender et al., 1994)
msl-1, like mle and H4Ac16 (an acetylated form of the His4 product), exhibits a wild type male localisation pattern in Sxl- XX nuclei.
(Palmer et al., 1994)
His4 protein is preferentially acetylated on Lys12 by HatB in vitro.
(Sobel et al., 1994)
The codon bias of the histone genes from D.melanogaster and D.hydei illustrates that the generalisation that abundantly expressed genes have a high codon bias and low rates of silent substitution does not hold for the histone genes.
(Fitch and Strausbaugh, 1993)
The position of the homologous histone gene repeats within the nuclei of early embryo cells has been investigated. The two homologous histone gene clusters are distinct and separate through all stages of the cell cycle up to nuclear cycle 13. During interphase of cycle 14, the two clusters colocalise with high frequency, and move from near the midline of the nucleus towards the apical side.
(Hiraoka et al., 1993)
TATA complex formation on the Hsp70Bb core promoter shows sequence dependence at the TATA element, at the transcription start site and further downstream. Similar interactions contribute to TATA complexes formed on the Hsp26 and His4 promoters.
(Purnell and Gilmour, 1993)
DNA replication of the 5kb histone gene repeating unit in tissue culture cells (Drosophila Kc cells) initiates at multiple sites located within the repeating unit. Several replication pause sites are located at 5' upstream regions of some histone genes.
(Shinomiya and Ina, 1993)
DNaseI footprinting analysis reveals core histones His2A, His2B, His3 and His4 (but not His1) bind to the kni, Kr and Ubx minimal enhancer elements in a periodic manner.
(Kerrigan and Kadonaga, 1992)
His4 protein isoforms acetylated at lysine residues 5, 8, 12, or 16 have been shown to have distinct patterns of distribution in interphase polytene chromosomes from larvae.
(Turner et al., 1992)
The pattern of His4 protein acetylation has been studied.
(Munks et al., 1991)
The genomic organisation of the histone genes in D.hydei closely resembles that of D.melanogaster.
(Kremer and Hennig, 1990)
The D.virilis core histone genes (Dvir\His2B, Dvir\His3, Dvir\His4 and Dvir\His2A), are arranged in the same order and orientation as the D.melanogaster core histone genes (His2B, His3, His4 and His2A). However, the His1 gene that is located between His2B and His3 in D.melanogaster is not found between Dvir\His2B and Dvir\His3 in D.virilis.
(Domier et al., 1986)
The expression of HIS-C genes, including His4, during oogenesis has been studied, and compared to periods of DNA synthesis and actin expression during this developmental stage.
(Ruddell and Jacobs-Lorena, 1985)
4.8kb and 5.0kb repeats containing the histone genes His1, His2A, His2B, His3 and His4 are present in all of the more than 20 D.melanogaster strains studied. The strains differ in the relative amounts of the two repeat types, with the 5.0kb repeat always present in equal or greater amounts than the 4.8kb repeat. The strains also differ in a number of far less abundant fragments containing histone gene sequences.
(Strausbaugh and Weinberg, 1982)
Encodes Histone H4. See HIS-C record.
 
hide External Crossreferences & Linkouts
Sequence Crossreferences
DDBJ / EMBL / GenBank
•
UniProtKB/Swiss-Prot
•
Other Crossreferences
InterPro domains - A database of protein families, domains, and functional sites
•
Histone H4 (IPR001951)
Histone core (IPR007125)
Histone-fold (IPR009072)
Histone H4, conserved site (IPR019809)
Linkouts
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
•
Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
•
hide Synonyms & Secondary IDs ( 17 )
Reported As
Symbol Synonym
4
(Rastelli and Kuroda, 1995)
Bin2
(Zhu and Hanes, 2000)
dH4
(Dominski et al., 2005)
DmeH4
(Fitch and Strausbaugh, 1993)
H4
(Cakouros et al., 2008, Sakaguchi et al., 2008, Camporeale et al., 2007, Varga-Weisz, 2006, Gunjan, 2006, Ivanovska et al., 2005, Hamada et al., 2005, Straub et al., 2005, Straub et al., 2005, Kusch et al., 2004, Kusch et al., 2004, Swaminathan et al., 2005, Karachentsev et al., 2005, Ebert et al., 2004, Larsson et al., 2004, Schaner et al., 2003, Qi et al., 2004, Frydrychova et al., 2005, Fu et al., 2004, Morales et al., 2004, Lippman and Martienssen, 2004, Schubeler et al., 2004, Schotta et al., 2004, Gilfillan et al., 2004, Aggarwal and Calvi, 2004, Aihara et al., 2004, Wang et al., 2004, Karachentsev and Steward, 2004, Hartl et al., 2004, Andersen and Panning, 2003, Loppin et al., 2001, Aggarwal and Calvi, 2003, Ketel et al., 2003, Cao et al., 2002, Beisel et al., 2002, Fang et al., 2002, Clapier et al., 2002, Krogan et al., 2002, Nishioka et al., 2002, Blower and Karpen, 2002, Meller and Rattner, 2002, Wassarman and Sauer, 2001, Levenstein and Kadonaga, 2002, Hamiche et al., 2001, Eissenberg, 2001, Berloco et al., 2001, Park and Kuroda, 2001, Smith et al., 2001, Katsani et al., 2001, Eberharter et al., 2001, Breiling et al., 2001, Nakagawa et al., 2001, Breiling et al., 2001, Wang et al., 2001, Birchler et al., 2001, Mello and Almouzni, 2001, Zaret and Wolffe, 2001, Aasland, 2001, Mizuguchi et al., 2001, Huang and Kadonaga, 2001, Wallrath, 2000, Ludlam et al., 2001, White-Cooper et al., 2001, Pile and Wassarman, 2000, Kelley and Kuroda, 2000, Turner, 2000, Mizzen and Allis, 2000, Pham and Sauer, 2000, Leach et al., 2000, Farkas et al., 2000, Akhtar et al., 2000, Verreault, 2000, Deuring et al., 2000, Johansen et al., 1999, Mahesh and Ranganath, 2000, Bhadra et al., 2000, Tyler et al., 1999, Kal et al., 2000, Zhu and Hanes, 2000, Gu et al., 2000, Grienenberger et al., 2000, Cavalli et al., 2000, Schutt and Nothiger, 2000, Tyler et al., 1999, Reim et al., 1999, Stuckenholz et al., 1999, Reim et al., 1999, Maurange et al., 1999, Kuroda, 1998, Hamiche et al., 1999, Adams and Kamakaka, 1999, Bhadra et al., 1999, Crane-Robinson and Wolffe, 1998, Carrier et al., 1999, Schienman et al., 1998, Borgnetto et al., 1999, Pollard and Peterson, 1998, Copps et al., 1998, Wallrath, 1998, Smith et al., 1998, Walker and Bownes, 1998, Rastelli and Kuroda, 1998, Eissenberg et al., 1998, Mizzen and Allis, 1998, Turner, 1998, Martinez-Balbas et al., 1998, Grunstein, 1997, Georgel et al., 1997, Hilfiker et al., 1997, Akhmanova et al., 1997, Anonymous, 1995, Strausbaugh and Williams, 1996, Cline and Meyer, 1996, Franke et al., 1996, Sobel et al., 1994, Xie et al., 1996, Blank and Becker, 1995, Rastelli et al., 1995, Granok et al., 1995, Sobel et al., 1995, Loidl, 1994, Franke and Baker, 1995, Gorman and Baker, 1994, Palmer et al., 1994, Soeller et al., 1993, Shinomiya and Ina, 1993, O'Brien and Lis, 1993, Papaceit and Juan, 1993, Kerrigan and Kadonaga, 1992, Becker and Wu, 1992, Pauli et al., 1992, Kas and Laemmli, 1992, Turner et al., 1992, Read and Manley, 1992, Shinomiya and Ina, 1991, O'Brien and Lis, 1991, Udvardy and Schedl, 1991, Munks et al., 1991, Harisanova et al., 1991, Harisanova and Ralchev, 1991, Kremer and Hennig, 1990, Amati and Gasser, 1990, Fitch et al., 1990, Domier et al., 1986, Ruddell and Jacobs-Lorena, 1985, Zhang et al., 2006, Grewal and Elgin, 2007, Mendjan et al., 2006, Wendt and Shilatifard, 2006, Krishnamoorthy et al., 2006, Deng and Meller, 2006, Demakova et al., 2007, Guelman et al., 2006, Maile et al., 2004, Papp and Muller, 2006, Ni et al., 2006, Prasanth and Spector, 2007, Furuhashi et al., 2006, Fortini, 2007, Jung and Bonini, 2007, Straub et al., 2005, Nowak et al., 2011, Canudas et al., 2005, Deng and Meller, 2006, Dominski et al., 2002, Adamson and Price, 2003, Prestel et al., 2010, Brasaemle and Hansen, 2006, Liu et al., 2006, Guelman et al., 2006, Birchler et al., 2006, Pal Bhadra et al., 2006, Secombe et al., 2007, Lanzotti et al., 2002, Ludlam et al., 2002, Birchler et al., 2008, Yin and Lin, 2007, Camporeale et al., 2006, Han et al., 2007, Li et al., 2002, Krejci and Bray, 2007, Isogai et al., 2007, Pankotai et al., 2005, Wang et al., 2006, Ciurciu et al., 2006, Tie et al., 2007, Andreyeva et al., 2007, Martinez and Arnosti, 2008, Li et al., 2008, Calvi et al., 2007, Park et al., 2007, Behm-Ansmant et al., 2007, Bell et al., 2007, Dalal et al., 2007, Ahlander et al., 2008, Deng et al., 2008, Corona et al., 2007, Beisel et al., 2007, Dalal et al., 2007, Andreyeva et al., 2005, Song et al., 2008, Font-Burgada et al., 2008, Rathke et al., 2007, Pindyurin et al., 2007, Yang et al., 2008, Fanti et al., 2008, Pile et al., 2002, Schwaiger et al., 2009, Graham et al., 2009, Scharf et al., 2009, Park et al., 2008, Sullivan et al., 2009, Grimm et al., 2009, Gorchakov et al., 2009, Plata et al., 2009, Gelbart et al., 2009, Pickersgill et al., 2006, Liu et al., 2008, Phalke et al., 2009, Grimm et al., 2007, Kulkarni-Shukla et al., 2008, Godfrey et al., 2006, Morciano et al., 2009, Zhang et al., 2010, Macalpine et al., 2010, Sawatsubashi et al., 2010, Lee et al., 2010, Zhang and Oliver, 2010, Corona et al., 2002, Scheuermann et al., 2010, Deal et al., 2010, Huang et al., 2010, Pinnola et al., 2007, Burgio et al., 2008, Lee et al., 2010, Orsi et al., 2010, Spain et al., 2010, Dubruille et al., 2010, Di Stefano et al., 2007, modENCODE Consortium et al., 2010, Spada et al., 2005, Bao et al., 2008, Larschan et al., 2011, Li and Arnosti, 2011, Regnard et al., 2011, Yu et al., 2010, Bonnefoy et al., 2007, Sullivan and Karpen, 2004, Lusser et al., 2005, Santoso and Kadonaga, 2006, Bell et al., 2010, Egelhofer et al., 2011, Kim et al., 2010, Moore et al., 2010, Guertin and Lis, 2010, Vatolina et al., 2011, Vatolina et al., 2011)
H4_DROME
(Storm and Sonnhammer, 2003)
H4Ac16
(Meller, 2000, Smith et al., 2001)
his
(Matsushima and Kaguni, 2007)
his4
(Wilkins and Lis, 1997)
His4
(Furuyama et al., 2006, Minakhina et al., 2003, Langille and Clark, 2007, Liu et al., 2005, Minidorff et al., 2007, Cakouros et al., 2008, Sakai et al., 2009, Kim and Marqués, 2010)
HisC
(Greil et al., 2003, van Steensel et al., 2001)
histone
(Corpet and Almouzni, 2007)
Name Synonym
Bicoid interacting protein 2
(Zhu and Hanes, 2000)
core histone
(Xia et al., 2003, Livengood et al., 2002)
histone
(Schwanbeck et al., 2004, Korber and Horz, 2004, Bao et al., 2004, Ishii et al., 2004, Duringer et al., 2003, Alexiadis et al., 2004, Matsushima et al., 2004, Kagansky et al., 2004, McKee, 2004, McBryant et al., 2003, Crevel et al., 2001, McKee et al., 2000, Donaghue et al., 2001, Crevel et al., 2001, Gemkow et al., 2001, Foe et al., 2000, Brent et al., 2000, Marley et al., 2000, Fitch and Wakimoto, 1998, Fung et al., 1998, Troyer et al., 1998, Baker et al., 1993, Machida et al., 2005, Wagner et al., 2008)
Histone
(Parsons et al., 2003, Breiling et al., 1999)
histone H4
(Moshkin et al., 2002, Marin et al., 2000, Aasland, 2000, Cavalli, 1999, Szuromi, 1999, Anonymous, 1994, Nibu et al., 2007, Sakaguchi and Steward, 2007, Jacquier et al., 2007, Parker et al., 2007, Rathke et al., 2007, Deng and Meller, 2006, Sakaguchi and Steward, 2007, Muller and Kassis, 2006, Lanzotti et al., 2002, Ludlam et al., 2002, Ringrose and Paro, 2007, Calvi et al., 2007, Kind et al., 2008, Hyllus et al., 2007, Cakouros et al., 2008, Ahlander et al., 2008, Karachentsev et al., 2007, Akhtar and Becker, 2001, Song et al., 2008, Rathke et al., 2007, Schwaiger et al., 2009, Corona et al., 2002, Pickersgill et al., 2006, Bulchand et al., 2010, Dubruille et al., 2010, Bao et al., 2008, Li and Arnosti, 2011)
Histone H4
(Papp and Muller, 2006, Wang et al., 2007, Scharf et al., 2009, Winkler et al., 2010, Yu et al., 2010)
Secondary FlyBase IDs
hide References ( 398 )
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hide Recent research papers ( 30 )
Egelhofer et al., 2011, Nat. Struct. Mol. Biol. 18(1): 91--93
An assessment of histone-modification antibody quality. [FBrf0212707]
Larschan et al., 2011, Nature 471(7336): 115--118
X chromosome dosage compensation via enhanced transcriptional elongation in Drosophila. [FBrf0213143]
Li and Arnosti, 2011, Curr. Biol. 21(5): 406--412
Long- and short-range transcriptional repressors induce distinct chromatin States on repressed genes. [FBrf0213170]
Nowak et al., 2011, J. Biol. Chem. 286(26): 23388--23396
Chromatin-modifying Complex Component Nurf55/p55 Associates with Histones H3 and H4 and Polycomb Repressive Complex 2 Subunit Su(z)12 through Partially Overlapping Binding Sites. [FBrf0213994]
Regnard et al., 2011, PLoS Genet. 7(3): e1001327
Global Analysis of the Relationship between JIL-1 Kinase and Transcription. [FBrf0213276]
Vatolina et al., 2011, Genetika, Moscow 47(5): 597--609
[Identification and molecular genetic characterization of the polytene chromosome interbands in Drosophila melanogaster]. [FBrf0214456]
Vatolina et al., 2011, Russ. J. Genet. 47(5): 521--532
Identification and molecular genetic characterization of the polytene chromosome interbands in Drosophila melanogaster. [FBrf0216692]
Bell et al., 2010, Nat. Struct. Mol. Biol. 17(7): 894--900
Accessibility of the Drosophila genome discriminates PcG repression, H4K16 acetylation and replication timing. [FBrf0211183]
Bulchand et al., 2010, J. Cell Sci. 123(16): 2697--2707
Muscle wasted: a novel component of the Drosophila histone locus body required for muscle integrity. [FBrf0211459]
Deal et al., 2010, Science 328(5982): 1161--1164
Genome-wide kinetics of nucleosome turnover determined by metabolic labeling of histones. [FBrf0210910]
Dubruille et al., 2010, Curr. Biol. 20(23): 2090--2099
Specialization of a Drosophila Capping Protein Essential for the Protection of Sperm Telomeres. [FBrf0212516]
Guertin and Lis, 2010, PLoS Genet. 6(9):
Chromatin Landscape Dictates HSF Binding to Target DNA Elements. [FBrf0211835]
Huang et al., 2010, J. Cell Sci. 123(16): 2853--2861
Drosophila CAF-1 regulates HP1-mediated epigenetic silencing and pericentric heterochromatin stability. [FBrf0211452]
Jung et al., 2010, Genomics 96(3): 154--166
Identification of conserved Drosophila-specific euchromatin-restricted non-coding sequence motifs. [FBrf0211521]
Kim and Marqués, 2010, Dev. Dyn. 239(9): 2413--2425
Identification of downstream targets of the Bone Morphogenetic Protein pathway in the Drosophila nervous system. [FBrf0211763]
Kim et al., 2010, Nat. Struct. Mol. Biol. 17(8): 1027--1029
Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. [FBrf0214093]
Lee et al., 2010, J. Biol. Chem. 285(12): 9041--9053
Drosophila octamer elements and pdm-1 dictate the coordinated transcription of core histone genes. [FBrf0210215]
Lee et al., 2010, Mol. Cell. Biol. 30(10): 2563--2577
Drosophila RB proteins repress differentiation-specific genes via two different mechanisms. [FBrf0210656]
Macalpine et al., 2010, Genome Res. 20(2): 201--211
Drosophila ORC localizes to open chromatin and marks sites of cohesin complex loading. [FBrf0209851]
modENCODE Consortium et al., 2010, Science 330(6012): 1787--1797
Identification of functional elements and regulatory circuits by Drosophila modENCODE. [FBrf0212741]
Moore et al., 2010, J. Biol. Chem. 285(52): 40879--40890
Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4. [FBrf0212637]
Orsi et al., 2010, J. Cell Sci. 123(20): 3515--3524
Drosophila I-R hybrid dysgenesis is associated with catastrophic meiosis and abnormal zygote formation. [FBrf0212012]
Prestel et al., 2010, Mol. Cell 38(6): 815--826
The Activation Potential of MOF Is Constrained for Dosage Compensation. [FBrf0211211]
Sawatsubashi et al., 2010, Genes Dev. 24(2): 159--170
A histone chaperone, DEK, transcriptionally coactivates a nuclear receptor. [FBrf0209754]
Scheuermann et al., 2010, Nature 465(7295): 243--247
Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB. [FBrf0210760]
Spain et al., 2010, J. Biol. Chem. 285(35): 27457--27467
Drosophila SIN3 isoforms interact with distinct proteins and have unique biological functions. [FBrf0211588]
Winkler et al., 2010, PLoS ONE 5(4): e10166
Groucho-mediated repression may result from a histone deacetylase-dependent increase in nucleosome density. [FBrf0210549]
Yu et al., 2010, genesis 48(3): 161--170
E(nos)/CG4699 required for nanos function in the female germ line of Drosophila. [FBrf0210233]
Zhang et al., 2010, PLoS Biol. 8(2): e1000320
Expression in aneuploid Drosophila s2 cells. [FBrf0210115]
Zhang and Oliver, 2010, BMC Genomics 11: 6
An evolutionary consequence of dosage compensation on Drosophila melanogaster female X-chromatin structure? [FBrf0209958]
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