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Gag proteins of the two Drosophila telomeric retrotransposons are targeted to chromosome ends
Drosophila telomeres are formed by two non-LTR retrotransposons, HeT-A and TART, which transpose only to chromosome ends. Successive transpositions of these telomeric elements yield arrays that are functionally equivalent to the arrays generated by telomerase in other organisms. In contrast, other D...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2002
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173066/ https://www.ncbi.nlm.nih.gov/pubmed/12417578 http://dx.doi.org/10.1083/jcb.200205039 |
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author | Rashkova, Svetlana Karam, Sarah E. Kellum, Rebecca Pardue, Mary-Lou |
author_facet | Rashkova, Svetlana Karam, Sarah E. Kellum, Rebecca Pardue, Mary-Lou |
author_sort | Rashkova, Svetlana |
collection | PubMed |
description | Drosophila telomeres are formed by two non-LTR retrotransposons, HeT-A and TART, which transpose only to chromosome ends. Successive transpositions of these telomeric elements yield arrays that are functionally equivalent to the arrays generated by telomerase in other organisms. In contrast, other Drosophila non-LTR retrotransposons transpose widely through gene-rich regions, but not to ends. The two telomeric elements encode very similar Gag proteins, suggesting that Gag may be involved in their unique targeting to chromosome ends. To test the intrinsic potential of these Gag proteins for targeting, we tagged the coding sequences with sequence of GFP and expressed the constructs in transiently transfected Drosophila-cultured cells. Gag proteins from both elements are efficiently transported into the nucleus where the protein from one element, HeT-A, forms structures associated with chromosome ends in interphase nuclei. Gag from the second element, TART, moves into telomere-associated structures only when coexpressed with HeT-A Gag. The results suggest that these Gag proteins are capable of delivering the retrotransposons to telomeres, although TART requires assistance from HeT-A. They also imply a symbiotic relationship between the two elements, with HeT-A Gag directing the telomere-specific targeting of the elements, whereas TART provides reverse transcriptase for transposition. |
format | Text |
id | pubmed-2173066 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21730662008-05-01 Gag proteins of the two Drosophila telomeric retrotransposons are targeted to chromosome ends Rashkova, Svetlana Karam, Sarah E. Kellum, Rebecca Pardue, Mary-Lou J Cell Biol Report Drosophila telomeres are formed by two non-LTR retrotransposons, HeT-A and TART, which transpose only to chromosome ends. Successive transpositions of these telomeric elements yield arrays that are functionally equivalent to the arrays generated by telomerase in other organisms. In contrast, other Drosophila non-LTR retrotransposons transpose widely through gene-rich regions, but not to ends. The two telomeric elements encode very similar Gag proteins, suggesting that Gag may be involved in their unique targeting to chromosome ends. To test the intrinsic potential of these Gag proteins for targeting, we tagged the coding sequences with sequence of GFP and expressed the constructs in transiently transfected Drosophila-cultured cells. Gag proteins from both elements are efficiently transported into the nucleus where the protein from one element, HeT-A, forms structures associated with chromosome ends in interphase nuclei. Gag from the second element, TART, moves into telomere-associated structures only when coexpressed with HeT-A Gag. The results suggest that these Gag proteins are capable of delivering the retrotransposons to telomeres, although TART requires assistance from HeT-A. They also imply a symbiotic relationship between the two elements, with HeT-A Gag directing the telomere-specific targeting of the elements, whereas TART provides reverse transcriptase for transposition. The Rockefeller University Press 2002-11-11 /pmc/articles/PMC2173066/ /pubmed/12417578 http://dx.doi.org/10.1083/jcb.200205039 Text en Copyright © 2002, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Report Rashkova, Svetlana Karam, Sarah E. Kellum, Rebecca Pardue, Mary-Lou Gag proteins of the two Drosophila telomeric retrotransposons are targeted to chromosome ends |
title | Gag proteins of the two Drosophila telomeric retrotransposons are targeted to chromosome ends |
title_full | Gag proteins of the two Drosophila telomeric retrotransposons are targeted to chromosome ends |
title_fullStr | Gag proteins of the two Drosophila telomeric retrotransposons are targeted to chromosome ends |
title_full_unstemmed | Gag proteins of the two Drosophila telomeric retrotransposons are targeted to chromosome ends |
title_short | Gag proteins of the two Drosophila telomeric retrotransposons are targeted to chromosome ends |
title_sort | gag proteins of the two drosophila telomeric retrotransposons are targeted to chromosome ends |
topic | Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173066/ https://www.ncbi.nlm.nih.gov/pubmed/12417578 http://dx.doi.org/10.1083/jcb.200205039 |
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