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Cohesin Rings Devoid of Scc3 and Pds5 Maintain Their Stable Association with the DNA
Cohesin is a protein complex that forms a ring around sister chromatids thus holding them together. The ring is composed of three proteins: Smc1, Smc3 and Scc1. The roles of three additional proteins that associate with the ring, Scc3, Pds5 and Wpl1, are not well understood. It has been proposed tha...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3415457/ https://www.ncbi.nlm.nih.gov/pubmed/22912589 http://dx.doi.org/10.1371/journal.pgen.1002856 |
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author | Kulemzina, Irina Schumacher, Martin R. Verma, Vikash Reiter, Jochen Metzler, Janina Failla, Antonio Virgilio Lanz, Christa Sreedharan, Vipin T. Rätsch, Gunnar Ivanov, Dmitri |
author_facet | Kulemzina, Irina Schumacher, Martin R. Verma, Vikash Reiter, Jochen Metzler, Janina Failla, Antonio Virgilio Lanz, Christa Sreedharan, Vipin T. Rätsch, Gunnar Ivanov, Dmitri |
author_sort | Kulemzina, Irina |
collection | PubMed |
description | Cohesin is a protein complex that forms a ring around sister chromatids thus holding them together. The ring is composed of three proteins: Smc1, Smc3 and Scc1. The roles of three additional proteins that associate with the ring, Scc3, Pds5 and Wpl1, are not well understood. It has been proposed that these three factors form a complex that stabilizes the ring and prevents it from opening. This activity promotes sister chromatid cohesion but at the same time poses an obstacle for the initial entrapment of sister DNAs. This hindrance to cohesion establishment is overcome during DNA replication via acetylation of the Smc3 subunit by the Eco1 acetyltransferase. However, the full mechanistic consequences of Smc3 acetylation remain unknown. In the current work, we test the requirement of Scc3 and Pds5 for the stable association of cohesin with DNA. We investigated the consequences of Scc3 and Pds5 depletion in vivo using degron tagging in budding yeast. The previously described DHFR–based N-terminal degron as well as a novel Eco1-derived C-terminal degron were employed in our study. Scc3 and Pds5 associate with cohesin complexes independently of each other and require the Scc1 “core” subunit for their association with chromosomes. Contrary to previous data for Scc1 downregulation, depletion of either Scc3 or Pds5 had a strong effect on sister chromatid cohesion but not on cohesin binding to DNA. Quantity, stability and genome-wide distribution of cohesin complexes remained mostly unchanged after the depletion of Scc3 and Pds5. Our findings are inconsistent with a previously proposed model that Scc3 and Pds5 are cohesin maintenance factors required for cohesin ring stability or for maintaining its association with DNA. We propose that Scc3 and Pds5 specifically function during cohesion establishment in S phase. |
format | Online Article Text |
id | pubmed-3415457 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34154572012-08-21 Cohesin Rings Devoid of Scc3 and Pds5 Maintain Their Stable Association with the DNA Kulemzina, Irina Schumacher, Martin R. Verma, Vikash Reiter, Jochen Metzler, Janina Failla, Antonio Virgilio Lanz, Christa Sreedharan, Vipin T. Rätsch, Gunnar Ivanov, Dmitri PLoS Genet Research Article Cohesin is a protein complex that forms a ring around sister chromatids thus holding them together. The ring is composed of three proteins: Smc1, Smc3 and Scc1. The roles of three additional proteins that associate with the ring, Scc3, Pds5 and Wpl1, are not well understood. It has been proposed that these three factors form a complex that stabilizes the ring and prevents it from opening. This activity promotes sister chromatid cohesion but at the same time poses an obstacle for the initial entrapment of sister DNAs. This hindrance to cohesion establishment is overcome during DNA replication via acetylation of the Smc3 subunit by the Eco1 acetyltransferase. However, the full mechanistic consequences of Smc3 acetylation remain unknown. In the current work, we test the requirement of Scc3 and Pds5 for the stable association of cohesin with DNA. We investigated the consequences of Scc3 and Pds5 depletion in vivo using degron tagging in budding yeast. The previously described DHFR–based N-terminal degron as well as a novel Eco1-derived C-terminal degron were employed in our study. Scc3 and Pds5 associate with cohesin complexes independently of each other and require the Scc1 “core” subunit for their association with chromosomes. Contrary to previous data for Scc1 downregulation, depletion of either Scc3 or Pds5 had a strong effect on sister chromatid cohesion but not on cohesin binding to DNA. Quantity, stability and genome-wide distribution of cohesin complexes remained mostly unchanged after the depletion of Scc3 and Pds5. Our findings are inconsistent with a previously proposed model that Scc3 and Pds5 are cohesin maintenance factors required for cohesin ring stability or for maintaining its association with DNA. We propose that Scc3 and Pds5 specifically function during cohesion establishment in S phase. Public Library of Science 2012-08-09 /pmc/articles/PMC3415457/ /pubmed/22912589 http://dx.doi.org/10.1371/journal.pgen.1002856 Text en © 2012 Kulemzina et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Kulemzina, Irina Schumacher, Martin R. Verma, Vikash Reiter, Jochen Metzler, Janina Failla, Antonio Virgilio Lanz, Christa Sreedharan, Vipin T. Rätsch, Gunnar Ivanov, Dmitri Cohesin Rings Devoid of Scc3 and Pds5 Maintain Their Stable Association with the DNA |
title | Cohesin Rings Devoid of Scc3 and Pds5 Maintain Their Stable Association with the DNA |
title_full | Cohesin Rings Devoid of Scc3 and Pds5 Maintain Their Stable Association with the DNA |
title_fullStr | Cohesin Rings Devoid of Scc3 and Pds5 Maintain Their Stable Association with the DNA |
title_full_unstemmed | Cohesin Rings Devoid of Scc3 and Pds5 Maintain Their Stable Association with the DNA |
title_short | Cohesin Rings Devoid of Scc3 and Pds5 Maintain Their Stable Association with the DNA |
title_sort | cohesin rings devoid of scc3 and pds5 maintain their stable association with the dna |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3415457/ https://www.ncbi.nlm.nih.gov/pubmed/22912589 http://dx.doi.org/10.1371/journal.pgen.1002856 |
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