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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...

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Autores principales: Takács, Sándor, Biessmann, Harald, Reddy, Hemakumar M., Mason, James M., Török, Tibor
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Ivyspring International Publisher 2012
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.
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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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