Literature DB >> 23723239

A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C.

Hidenori Kato1, Jiansheng Jiang, Bing-Rui Zhou, Marieke Rozendaal, Hanqiao Feng, Rodolfo Ghirlando, T Sam Xiao, Aaron F Straight, Yawen Bai.   

Abstract

Chromosome segregation during mitosis requires assembly of the kinetochore complex at the centromere. Kinetochore assembly depends on specific recognition of the histone variant CENP-A in the centromeric nucleosome by centromere protein C (CENP-C). We have defined the determinants of this recognition mechanism and discovered that CENP-C binds a hydrophobic region in the CENP-A tail and docks onto the acidic patch of histone H2A and H2B. We further found that the more broadly conserved CENP-C motif uses the same mechanism for CENP-A nucleosome recognition. Our findings reveal a conserved mechanism for protein recruitment to centromeres and a histone recognition mode whereby a disordered peptide binds the histone tail through hydrophobic interactions facilitated by nucleosome docking.

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Year:  2013        PMID: 23723239      PMCID: PMC3763809          DOI: 10.1126/science.1235532

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  28 in total

1.  CCAN makes multiple contacts with centromeric DNA to provide distinct pathways to the outer kinetochore.

Authors:  Tetsuya Hori; Miho Amano; Aussie Suzuki; Chelsea B Backer; Julie P Welburn; Yimin Dong; Bruce F McEwen; Wei-Hao Shang; Emiko Suzuki; Katsuya Okawa; Iain M Cheeseman; Tatsuo Fukagawa
Journal:  Cell       Date:  2008-12-12       Impact factor: 41.582

2.  Dissection of CENP-C-directed centromere and kinetochore assembly.

Authors:  Kirstin J Milks; Ben Moree; Aaron F Straight
Journal:  Mol Biol Cell       Date:  2009-07-29       Impact factor: 4.138

3.  CENP-C functions as a scaffold for effectors with essential kinetochore functions in mitosis and meiosis.

Authors:  Koichi Tanaka; Hui Li Chang; Ayano Kagami; Yoshinori Watanabe
Journal:  Dev Cell       Date:  2009-09       Impact factor: 12.270

4.  CENP-C is a structural platform for kinetochore assembly.

Authors:  Marcin R Przewloka; Zsolt Venkei; Victor M Bolanos-Garcia; Janusz Debski; Michal Dadlez; David M Glover
Journal:  Curr Biol       Date:  2011-02-25       Impact factor: 10.834

Review 5.  Centromeres: unique chromatin structures that drive chromosome segregation.

Authors:  Jolien S Verdaasdonk; Kerry Bloom
Journal:  Nat Rev Mol Cell Biol       Date:  2011-05       Impact factor: 94.444

6.  Epigenetic centromere propagation and the nature of CENP-a nucleosomes.

Authors:  Ben E Black; Don W Cleveland
Journal:  Cell       Date:  2011-02-18       Impact factor: 41.582

7.  Dual recognition of CENP-A nucleosomes is required for centromere assembly.

Authors:  Christopher W Carroll; Kirstin J Milks; Aaron F Straight
Journal:  J Cell Biol       Date:  2010-06-21       Impact factor: 10.539

8.  Structural and functional dissection of Mif2p, a conserved DNA-binding kinetochore protein.

Authors:  R L Cohen; C W Espelin; P De Wulf; P K Sorger; S C Harrison; K T Simons
Journal:  Mol Biol Cell       Date:  2008-08-13       Impact factor: 4.138

9.  Direct binding of Cenp-C to the Mis12 complex joins the inner and outer kinetochore.

Authors:  Emanuela Screpanti; Anna De Antoni; Gregory M Alushin; Arsen Petrovic; Tiziana Melis; Eva Nogales; Andrea Musacchio
Journal:  Curr Biol       Date:  2011-02-25       Impact factor: 10.834

10.  Structure of RCC1 chromatin factor bound to the nucleosome core particle.

Authors:  Ravindra D Makde; Joseph R England; Hemant P Yennawar; Song Tan
Journal:  Nature       Date:  2010-08-25       Impact factor: 49.962

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  166 in total

1.  The CENP-L-N Complex Forms a Critical Node in an Integrated Meshwork of Interactions at the Centromere-Kinetochore Interface.

Authors:  Kara L McKinley; Nikolina Sekulic; Lucie Y Guo; Tonia Tsinman; Ben E Black; Iain M Cheeseman
Journal:  Mol Cell       Date:  2015-11-19       Impact factor: 17.970

2.  Homodimeric PHD Domain-containing Rco1 Subunit Constitutes a Critical Interaction Hub within the Rpd3S Histone Deacetylase Complex.

Authors:  Chun Ruan; Haochen Cui; Chul-Hwan Lee; Sheng Li; Bing Li
Journal:  J Biol Chem       Date:  2016-01-08       Impact factor: 5.157

Review 3.  Touch, act and go: landing and operating on nucleosomes.

Authors:  Valentina Speranzini; Simona Pilotto; Titia K Sixma; Andrea Mattevi
Journal:  EMBO J       Date:  2016-01-19       Impact factor: 11.598

Review 4.  The right place at the right time: chaperoning core histone variants.

Authors:  Francesca Mattiroli; Sheena D'Arcy; Karolin Luger
Journal:  EMBO Rep       Date:  2015-10-12       Impact factor: 8.807

5.  Swapping CENP-A at the centromere.

Authors:  Bradley T French; Aaron F Straight
Journal:  Nat Cell Biol       Date:  2013-09       Impact factor: 28.824

6.  Structural basis for histone H2B deubiquitination by the SAGA DUB module.

Authors:  Michael T Morgan; Mahmood Haj-Yahya; Alison E Ringel; Prasanthi Bandi; Ashraf Brik; Cynthia Wolberger
Journal:  Science       Date:  2016-02-12       Impact factor: 47.728

7.  Structures of CENP-C cupin domains at regional centromeres reveal unique patterns of dimerization and recruitment functions for the inner pocket.

Authors:  Jennifer K Chik; Vera Moiseeva; Pavitra K Goel; Ben A Meinen; Philipp Koldewey; Sojin An; Barbara G Mellone; Lakxmi Subramanian; Uhn-Soo Cho
Journal:  J Biol Chem       Date:  2019-07-31       Impact factor: 5.157

Review 8.  Nucleosome structure and dynamics are coming of age.

Authors:  Keda Zhou; Guillaume Gaullier; Karolin Luger
Journal:  Nat Struct Mol Biol       Date:  2018-12-10       Impact factor: 15.369

Review 9.  The kinetochore.

Authors:  Iain M Cheeseman
Journal:  Cold Spring Harb Perspect Biol       Date:  2014-07-01       Impact factor: 10.005

Review 10.  The centromere: epigenetic control of chromosome segregation during mitosis.

Authors:  Frederick G Westhorpe; Aaron F Straight
Journal:  Cold Spring Harb Perspect Biol       Date:  2014-11-20       Impact factor: 10.005

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