A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Dmel\HeT-A

General Information
Symbol Dmel\HeT-A Species D.melanogaster
Name HeT-A element FlyBase ID FBte0000143
Feature type natural transposable element
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Description
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FB2013_03
FB2013_02
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Complete element (bp)
Terminal repeat (bp)
Reference sequence transposon_sequence_set.embl.txt.gz
Component genes
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Transposon type
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Copy number
and comments
3 in euchromatin of Release 3 genome annotation, of which zero are full length.
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Target Site Duplication
Size (bp)
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Curated drosophilid orthologs
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HeT-A and TART-element, previously considered to be closely related, have very different transcriptional characteristics. Additionally, features of TART-element sequence organisation resemble those of a subclass of non-LTR elements characterized by unequal terminal repeats. The distinctive transcription patterns of HeT-A and TART-element are conserved in D.yakuba.
HeT-A sequences have been found in the centric heterochromatin of chromosome 3.
The HeT-A promoter is at the 3' end of the element and directs transcription of the HeT-A element immediately downstream in the tandem array in which they are found. The HeT-A element appears to be an evolutionary intermediate between LTR and non-LTR retrotransposons. Considering two HeT-A elements in tandem array, the promoter-containing 3' end of the upstream element is identical to the promoter-containing 3' end of the downstream element, and this "extended element" is structurally and functionally equivalent to an LTR retrotransposon. The promoter-containing 3' end of the upstream element acts as a surrogate for the 5' LTR characteristic of the LTR retrotransposon, although it is actually part of the flanking element. The HeT-A element does not encode its own reverse transcriptase.
Comparison of integrase/transposase domains to new elements containing the DDE signature.
HeT-A promoter activity is located in the 3' end of the element. In HeT-A arrays the 3' sequence of one element directs transcription of its downstream neighbour.
HeT-A retrotransposons hybridise close to the centromere of the Y chromosome.
HeT-A element and TART-element may be evolutionarily related to telomerase, in both cases an enzyme extends the end of a chromosome by adding DNA copied from an RNA template.
A HeT-A element has been cloned and sequenced. The unit length of the HeT-A element is approximately 6kb.
The HeT-A element is approximately 6kb in length. It can be divided into three regions; a protein coding region composed of two overlapping reading frames, a 5' non-coding region and a 3' non-coding region (which makes up approximately half the HeT-A element).
Analysis of HeT-A transcripts suggests that HeT-A elements transposase by means of a polyadenylated RNA intermediate and that each element joins to the chromosome end by means of the poly(A) tail of the RNA.
The genomic organization (oligo(A) tails facing proximally at chromosome ends) and sequence analysis of 29 different HeT-A fragments supports the model of telomere elongation by transposition of HeT-A elements.
HeT-A sequences are never found in the euchromatin. Y associated HeT-A clusters have significantly different structures than telomeric clusters, and may arise by different transposition mechanisms.
A transposon family of non-long terminal repeat retrotransposons found at the telomere. HeT-A elements transpose to broken chromosome ends. Evidence suggests that they can also transpose to natural chromosome ends.
HeT-A is a transposable element that heals broken chromosomes: it may have a structural role in telomere organization or maintenance.
Transposition of HeT-A onto broken chromosome ends is implicated in chromosome healing. Ends of X chromosomes with new HeT-A additions receded at the same rate as broken ends before HeT-A elements attached. Approximately 1% of chromosomes per generation aquired new HeT-A sequences of an average of 6kb at their ends, and the rate of addition of new material per generation matches the observed rate of loss caused by incomplete replication at the ends of the DNA molecule. Transposition of HeT-A onto broken chromosome ends is implicated in chromosome healing. Ends of X chromosomes with new HeT-A additions receded at the same rate as broken ends before HeT-A elements attached. Approximately 1% of chromosomes per generation aquired new HeT-A sequences of an average of 6kb at their ends, and the rate of addition of new material per generation matches the observed rate of loss caused by incomplete replication at the ends of the DNA molecule.
Sequence of a HeT-A element includes two overlapping open reading frames that are one nucleotide out of frame with respect to each other. The longer ORF contains Cys-His motifs strongly resembling nucleic acid binding domains of gag-like proteins and the overall organisation is reminiscent of LINE elements.
HeT-As is transcribed and are conserved in the D.melanogaster species subgroup. It may play a role in the structure and/or function of telomeres.
construct_comment: Associated with telomeres.
The distribution of different subfragments of HeT-A DNA throughout the genome has been studied.
HeT-A may have a role in organizing or maintaining the ends of chromosomes. The association of HeT-A with the newly acquired telomeres, in a formerly euchromatic region of C(1)A, strengthens this correlation.
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hide Synonyms & Secondary IDs ( 15 )
Reported As
Symbol Synonym
Het
 
Telo3R
 
Name Synonym
HeT-A element
 
telomeric HeT-A element
Secondary FlyBase IDs
  • FBgn0004141
  • FBgn0004457
  • FBgn0010279
  • FBtp0011436
hide References ( 225 )
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hide Recent research papers ( 15 )
Anand and Kai, 2012, EMBO J. 31(4): 870--882
The tudor domain protein Kumo is required to assemble the nuage and to generate germline piRNAs in Drosophila. [FBrf0217541]
Olivieri et al., 2012, Mol. Cell 47(6): 954--969
The Cochaperone Shutdown Defines a Group of Biogenesis Factors Essential for All piRNA Populations in Drosophila. [FBrf0219572]
Preall et al., 2012, RNA 18(8): 1446--1457
shutdown is a component of the Drosophila piRNA biogenesis machinery. [FBrf0218942]
Sienski et al., 2012, Cell 151(5): 964--980
Transcriptional silencing of transposons by piwi and maelstrom and its impact on chromatin state and gene expression. [FBrf0220033]
Sreesankar et al., 2012, BMC Genomics 13: 255
Functional diversification of yeast telomere associated protein, Rif1, in higher eukaryotes. [FBrf0219090]
Takács et al., 2012, Int. J. Biol. Sci. 8(7): 1055--1061
Protein interactions on telomeric retrotransposons in Drosophila. [FBrf0219367]
Tan et al., 2012, Hum. Mol. Genet. 21(1): 57--65
Retrotransposon activation contributes to fragile X premutation rCGG-mediated neurodegeneration. [FBrf0216915]
Debaryshe and Pardue, 2011, Genetics 187(1): 51--60
Differential maintenance of DNA sequences in telomeric and centromeric heterochromatin. [FBrf0212756]
Handler et al., 2011, EMBO J. 30(19): 3977--3993
A systematic analysis of Drosophila TUDOR domain-containing proteins identifies Vreteno and the Tdrd12 family as essential primary piRNA pathway factors. [FBrf0216344]
Klenov et al., 2011, Proc. Natl. Acad. Sci. U.S.A. 108(46): 18760--18765
Separation of stem cell maintenance and transposon silencing functions of Piwi protein. [FBrf0216776]
Liu et al., 2011, Development 138(9): 1863--1873
PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition. [FBrf0213491]
Pane et al., 2011, EMBO J. 30(22): 4601--4615
The Cutoff protein regulates piRNA cluster expression and piRNA production in the Drosophila germline. [FBrf0217070]
Shpiz et al., 2011, Nucleic Acids Res. 39(20): 8703--8711
Mechanism of the piRNA-mediated silencing of Drosophila telomeric retrotransposons. [FBrf0216525]
Wang and Elgin, 2011, Proc. Natl. Acad. Sci. U.S.A. 108(52): 21164--21169
Drosophila Piwi functions downstream of piRNA production mediating a chromatin-based transposon silencing mechanism in female germ line. [FBrf0217081]
Zhang et al., 2011, Mol. Cell 44(4): 572--584
Heterotypic piRNA Ping-Pong Requires Qin, a Protein with Both E3 Ligase and Tudor Domains. [FBrf0216809]
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