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Interallelic complementation provides functional evidence for cohesin–cohesin interactions on DNA
The cohesin complex (Mcd1p, Smc1p, Smc3p, and Scc3p) has multiple roles in chromosome architecture, such as promoting sister chromatid cohesion, chromosome condensation, DNA repair, and transcriptional regulation. The prevailing embrace model for sister chromatid cohesion posits that a single cohesi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4642856/ https://www.ncbi.nlm.nih.gov/pubmed/26378250 http://dx.doi.org/10.1091/mbc.E15-06-0331 |
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author | Eng, Thomas Guacci, Vincent Koshland, Douglas |
author_facet | Eng, Thomas Guacci, Vincent Koshland, Douglas |
author_sort | Eng, Thomas |
collection | PubMed |
description | The cohesin complex (Mcd1p, Smc1p, Smc3p, and Scc3p) has multiple roles in chromosome architecture, such as promoting sister chromatid cohesion, chromosome condensation, DNA repair, and transcriptional regulation. The prevailing embrace model for sister chromatid cohesion posits that a single cohesin complex entraps both sister chromatids. We report interallelic complementation between pairs of nonfunctional mcd1 alleles (mcd1-1 and mcd1-Q266) or smc3 alleles (smc3-42 and smc3-K113R). Cells bearing individual mcd1 or smc3 mutant alleles are inviable and defective for both sister chromatid cohesion and condensation. However, cells coexpressing two defective mcd1 or two defective smc3 alleles are viable and have cohesion and condensation. Because cohesin contains only a single copy of Smc3p or Mcd1p, these examples of interallelic complementation must result from interplay or communication between the two defective cohesin complexes, each harboring one of the mutant allele products. Neither mcd1-1p nor smc3-42p is bound to chromosomes when expressed individually at its restrictive temperature. However, their chromosome binding is restored when they are coexpressed with their chromosome-bound interallelic complementing partner. Our results support a mechanism by which multiple cohesin complexes interact on DNA to mediate cohesion and condensation. |
format | Online Article Text |
id | pubmed-4642856 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-46428562016-01-30 Interallelic complementation provides functional evidence for cohesin–cohesin interactions on DNA Eng, Thomas Guacci, Vincent Koshland, Douglas Mol Biol Cell Articles The cohesin complex (Mcd1p, Smc1p, Smc3p, and Scc3p) has multiple roles in chromosome architecture, such as promoting sister chromatid cohesion, chromosome condensation, DNA repair, and transcriptional regulation. The prevailing embrace model for sister chromatid cohesion posits that a single cohesin complex entraps both sister chromatids. We report interallelic complementation between pairs of nonfunctional mcd1 alleles (mcd1-1 and mcd1-Q266) or smc3 alleles (smc3-42 and smc3-K113R). Cells bearing individual mcd1 or smc3 mutant alleles are inviable and defective for both sister chromatid cohesion and condensation. However, cells coexpressing two defective mcd1 or two defective smc3 alleles are viable and have cohesion and condensation. Because cohesin contains only a single copy of Smc3p or Mcd1p, these examples of interallelic complementation must result from interplay or communication between the two defective cohesin complexes, each harboring one of the mutant allele products. Neither mcd1-1p nor smc3-42p is bound to chromosomes when expressed individually at its restrictive temperature. However, their chromosome binding is restored when they are coexpressed with their chromosome-bound interallelic complementing partner. Our results support a mechanism by which multiple cohesin complexes interact on DNA to mediate cohesion and condensation. The American Society for Cell Biology 2015-11-15 /pmc/articles/PMC4642856/ /pubmed/26378250 http://dx.doi.org/10.1091/mbc.E15-06-0331 Text en © 2015 Eng et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Eng, Thomas Guacci, Vincent Koshland, Douglas Interallelic complementation provides functional evidence for cohesin–cohesin interactions on DNA |
title | Interallelic complementation provides functional evidence for cohesin–cohesin interactions on DNA |
title_full | Interallelic complementation provides functional evidence for cohesin–cohesin interactions on DNA |
title_fullStr | Interallelic complementation provides functional evidence for cohesin–cohesin interactions on DNA |
title_full_unstemmed | Interallelic complementation provides functional evidence for cohesin–cohesin interactions on DNA |
title_short | Interallelic complementation provides functional evidence for cohesin–cohesin interactions on DNA |
title_sort | interallelic complementation provides functional evidence for cohesin–cohesin interactions on dna |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4642856/ https://www.ncbi.nlm.nih.gov/pubmed/26378250 http://dx.doi.org/10.1091/mbc.E15-06-0331 |
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