Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing
Condensin is required for chromosome dynamics and diverse DNA metabolism. How condensin works, however, is not well understood. Condensin contains two structural maintenance of chromosomes (SMC) subunits with the terminal globular domains connected to coiled-coil that is interrupted by the central h...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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The Royal Society
2011-01-01
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| Series: | Open Biology |
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| Online Access: | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.110023 |
| _version_ | 1819315499596513280 |
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| author | Yuko Akai Yumiko Kurokawa Norihiko Nakazawa Yuko Tonami-Murakami Yuki Suzuki Shige H. Yoshimura Hiroshi Iwasaki Yoshiharu Shiroiwa Takahiro Nakamura Eri Shibata Mitsuhiro Yanagida |
| author_facet | Yuko Akai Yumiko Kurokawa Norihiko Nakazawa Yuko Tonami-Murakami Yuki Suzuki Shige H. Yoshimura Hiroshi Iwasaki Yoshiharu Shiroiwa Takahiro Nakamura Eri Shibata Mitsuhiro Yanagida |
| author_sort | Yuko Akai |
| collection | DOAJ |
| description | Condensin is required for chromosome dynamics and diverse DNA metabolism. How condensin works, however, is not well understood. Condensin contains two structural maintenance of chromosomes (SMC) subunits with the terminal globular domains connected to coiled-coil that is interrupted by the central hinge. Heterotrimeric non-SMC subunits regulate SMC. We identified a novel fission yeast SMC hinge mutant, cut14-Y1, which displayed defects in DNA damage repair and chromosome segregation. It contains an amino acid substitution at a conserved hinge residue of Cut14/SMC2, resulting in diminished DNA binding and annealing. A replication protein A mutant, ssb1-418, greatly alleviated the repair and mitotic defects of cut14-Y1. Ssb1 protein formed nucleolar foci in cut14-Y1 cells, but the number of foci was diminished in cut14-Y1 ssb1-418 double mutants. Consistent with the above results, Ssb1 protein bound to single-strand DNA was removed by condensin or the SMC dimer through DNA reannealing in vitro. Similarly, RNA hybridized to DNA may be removed by the SMC dimer. Thus, condensin may wind up DNA strands to unload chromosomal components after DNA repair and prior to mitosis. We show that 16 suppressor mutations of cut14-Y1 were all mapped within the hinge domain, which surrounded the original L543 mutation site. |
| first_indexed | 2024-12-24T10:01:05Z |
| format | Article |
| id | doaj.art-11f9309ed10b462d8468708a9a9d513f |
| institution | Directory Open Access Journal |
| issn | 2046-2441 |
| language | English |
| last_indexed | 2024-12-24T10:01:05Z |
| publishDate | 2011-01-01 |
| publisher | The Royal Society |
| record_format | Article |
| series | Open Biology |
| spelling | doaj.art-11f9309ed10b462d8468708a9a9d513f2022-12-21T17:01:01ZengThe Royal SocietyOpen Biology2046-24412011-01-011410.1098/rsob.110023110023Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealingYuko AkaiYumiko KurokawaNorihiko NakazawaYuko Tonami-MurakamiYuki SuzukiShige H. YoshimuraHiroshi IwasakiYoshiharu ShiroiwaTakahiro NakamuraEri ShibataMitsuhiro YanagidaCondensin is required for chromosome dynamics and diverse DNA metabolism. How condensin works, however, is not well understood. Condensin contains two structural maintenance of chromosomes (SMC) subunits with the terminal globular domains connected to coiled-coil that is interrupted by the central hinge. Heterotrimeric non-SMC subunits regulate SMC. We identified a novel fission yeast SMC hinge mutant, cut14-Y1, which displayed defects in DNA damage repair and chromosome segregation. It contains an amino acid substitution at a conserved hinge residue of Cut14/SMC2, resulting in diminished DNA binding and annealing. A replication protein A mutant, ssb1-418, greatly alleviated the repair and mitotic defects of cut14-Y1. Ssb1 protein formed nucleolar foci in cut14-Y1 cells, but the number of foci was diminished in cut14-Y1 ssb1-418 double mutants. Consistent with the above results, Ssb1 protein bound to single-strand DNA was removed by condensin or the SMC dimer through DNA reannealing in vitro. Similarly, RNA hybridized to DNA may be removed by the SMC dimer. Thus, condensin may wind up DNA strands to unload chromosomal components after DNA repair and prior to mitosis. We show that 16 suppressor mutations of cut14-Y1 were all mapped within the hinge domain, which surrounded the original L543 mutation site.https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.110023structural maintenance of chromosomesdna damagemitosisdna metabolismcondensation |
| spellingShingle | Yuko Akai Yumiko Kurokawa Norihiko Nakazawa Yuko Tonami-Murakami Yuki Suzuki Shige H. Yoshimura Hiroshi Iwasaki Yoshiharu Shiroiwa Takahiro Nakamura Eri Shibata Mitsuhiro Yanagida Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing Open Biology structural maintenance of chromosomes dna damage mitosis dna metabolism condensation |
| title | Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing |
| title_full | Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing |
| title_fullStr | Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing |
| title_full_unstemmed | Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing |
| title_short | Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing |
| title_sort | opposing role of condensin hinge against replication protein a in mitosis and interphase through promoting dna annealing |
| topic | structural maintenance of chromosomes dna damage mitosis dna metabolism condensation |
| url | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.110023 |
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