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Protein Interactions on Telomeric Retrotransposons in Drosophila
Telomere length in Drosophila is maintained by targeted transposition of three non-LTR retrotransposons: HeT-A, TART and TAHRE (HTT), but understanding the regulation of this process is hindered by our poor knowledge of HTT associated proteins. We have identified new protein components of the HTT ar...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Ivyspring International Publisher
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432853/ https://www.ncbi.nlm.nih.gov/pubmed/22949888 http://dx.doi.org/10.7150/ijbs.4460 |
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author | Takács, Sándor Biessmann, Harald Reddy, Hemakumar M. Mason, James M. Török, Tibor |
author_facet | Takács, Sándor Biessmann, Harald Reddy, Hemakumar M. Mason, James M. Török, Tibor |
author_sort | Takács, Sándor |
collection | PubMed |
description | Telomere length in Drosophila is maintained by targeted transposition of three non-LTR retrotransposons: HeT-A, TART and TAHRE (HTT), but understanding the regulation of this process is hindered by our poor knowledge of HTT associated proteins. We have identified new protein components of the HTT array: Chromator (Chro), the TRF2/DREF complex and the sumoylation machinery. Chro was localized on telomeric HTT arrays by immunostaining, where it may interact with Prod directly, as indicated by yeast two-hybrid interaction, co-IP, and colocalization on polytene chromosomes. The TRF2/DREF complex may promote the open structure of HTT chromatin. The protein interactions controlling HTT chromatin structure and telomere length may be modulated by sumoylation. |
format | Online Article Text |
id | pubmed-3432853 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Ivyspring International Publisher |
record_format | MEDLINE/PubMed |
spelling | pubmed-34328532012-09-04 Protein Interactions on Telomeric Retrotransposons in Drosophila Takács, Sándor Biessmann, Harald Reddy, Hemakumar M. Mason, James M. Török, Tibor Int J Biol Sci Short Research Communication Telomere length in Drosophila is maintained by targeted transposition of three non-LTR retrotransposons: HeT-A, TART and TAHRE (HTT), but understanding the regulation of this process is hindered by our poor knowledge of HTT associated proteins. We have identified new protein components of the HTT array: Chromator (Chro), the TRF2/DREF complex and the sumoylation machinery. Chro was localized on telomeric HTT arrays by immunostaining, where it may interact with Prod directly, as indicated by yeast two-hybrid interaction, co-IP, and colocalization on polytene chromosomes. The TRF2/DREF complex may promote the open structure of HTT chromatin. The protein interactions controlling HTT chromatin structure and telomere length may be modulated by sumoylation. Ivyspring International Publisher 2012-08-15 /pmc/articles/PMC3432853/ /pubmed/22949888 http://dx.doi.org/10.7150/ijbs.4460 Text en © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited. |
spellingShingle | Short Research Communication Takács, Sándor Biessmann, Harald Reddy, Hemakumar M. Mason, James M. Török, Tibor Protein Interactions on Telomeric Retrotransposons in Drosophila |
title | Protein Interactions on Telomeric Retrotransposons in Drosophila |
title_full | Protein Interactions on Telomeric Retrotransposons in Drosophila |
title_fullStr | Protein Interactions on Telomeric Retrotransposons in Drosophila |
title_full_unstemmed | Protein Interactions on Telomeric Retrotransposons in Drosophila |
title_short | Protein Interactions on Telomeric Retrotransposons in Drosophila |
title_sort | protein interactions on telomeric retrotransposons in drosophila |
topic | Short Research Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432853/ https://www.ncbi.nlm.nih.gov/pubmed/22949888 http://dx.doi.org/10.7150/ijbs.4460 |
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