Recognition of centromere-specific histone Cse4 by the inner kinetochore Okp1-Ame1 complex.


Journal

EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049

Informations de publication

Date de publication:
06 Dec 2023
Historique:
revised: 30 10 2023
received: 21 06 2023
accepted: 02 11 2023
medline: 11 12 2023
pubmed: 20 11 2023
entrez: 20 11 2023
Statut: ppublish

Résumé

Successful mitosis depends on the timely establishment of correct chromosomal attachments to microtubules. The kinetochore, a modular multiprotein complex, mediates this connection by recognizing specialized chromatin containing a histone H3 variant called Cse4 in budding yeast and CENP-A in vertebrates. Structural features of the kinetochore that enable discrimination between Cse4/CENP-A and H3 have been identified in several species. How and when these contribute to centromere recognition and how they relate to the overall structure of the inner kinetochore are unsettled questions. More generally, this molecular recognition ensures that only one kinetochore is built on each chromatid and that this happens at the right place on the chromatin fiber. We have determined the crystal structure of a Cse4 peptide bound to the essential inner kinetochore Okp1-Ame1 heterodimer from budding yeast. The structure and related experiments show in detail an essential point of Cse4 contact and provide information about the arrangement of the inner kinetochore.

Identifiants

pubmed: 37983946
doi: 10.15252/embr.202357702
pmc: PMC10702835
doi:

Substances chimiques

Histones 0
Centromere Protein A 0
Saccharomyces cerevisiae Proteins 0
Chromosomal Proteins, Non-Histone 0
DNA-Binding Proteins 0
Cell Cycle Proteins 0
Chromatin 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e57702

Subventions

Organisme : NIGMS NIH HHS
ID : P30 GM124165
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM116897
Pays : United States

Informations de copyright

© 2023 The Authors. Published under the terms of the CC BY 4.0 license.

Références

Elife. 2018 Aug 23;7:
pubmed: 30136924
EMBO Rep. 2023 Dec 6;24(12):e57702
pubmed: 37983946
Mol Cell. 2010 Nov 12;40(3):444-54
pubmed: 21070970
Sci Adv. 2023 Jul 28;9(30):eadg7480
pubmed: 37506202
Mol Biol Cell. 2013 Jun;24(12):2034-44
pubmed: 23637466
J Biol Chem. 2016 Apr 15;291(16):8825-35
pubmed: 26921322
Protein Sci. 2022 Jan;31(1):232-250
pubmed: 34747533
Acta Crystallogr D Biol Crystallogr. 2013 Jul;69(Pt 7):1204-14
pubmed: 23793146
Cell Cycle. 2005 Oct;4(10):1448-56
pubmed: 16177574
Proc Natl Acad Sci U S A. 2012 Jun 5;109(23):9029-34
pubmed: 22615363
Mol Cell. 2010 Nov 12;40(3):455-64
pubmed: 21070971
G3 (Bethesda). 2018 Mar 28;8(4):1215-1223
pubmed: 29432128
Genes Dev. 2003 Dec 1;17(23):2902-21
pubmed: 14633972
Elife. 2019 May 21;8:
pubmed: 31112132
EMBO J. 2019 Jan 3;38(1):
pubmed: 30389668
Curr Biol. 2020 Sep 7;30(17):3425-3431.e3
pubmed: 32679099
Genes Dev. 1999 May 1;13(9):1140-55
pubmed: 10323865
Nature. 2019 Oct;574(7777):278-282
pubmed: 31578520
Mol Cell Biol. 2000 Sep;20(18):7037-48
pubmed: 10958698
Nat Struct Mol Biol. 2018 Dec;25(12):1103-1110
pubmed: 30478265
J Cell Biol. 2014 Aug 18;206(4):509-24
pubmed: 25135934
Structure. 2020 Mar 3;28(3):363-370.e3
pubmed: 32004465
Cell. 2002 Oct 18;111(2):163-72
pubmed: 12408861
Elife. 2019 Feb 14;8:
pubmed: 30762520
Nat Commun. 2021 Mar 19;12(1):1763
pubmed: 33741944
Nature. 2021 Aug;596(7873):583-589
pubmed: 34265844
Cell. 2016 Nov 3;167(4):1014-1027.e12
pubmed: 27881300
Mol Biol Cell. 2021 Nov 1;32(21):ar15
pubmed: 34432494
Curr Biol. 2023 Feb 27;33(4):688-696.e6
pubmed: 36736323
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
pubmed: 20383002
EMBO J. 2017 Dec 1;36(23):3458-3482
pubmed: 29046335
Elife. 2020 May 14;9:
pubmed: 32406818
Methods Mol Biol. 2014;1205:13-28
pubmed: 25213236
FEMS Yeast Res. 2018 Feb 1;18(1):
pubmed: 29272409
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21
pubmed: 20124702
Elife. 2014 May 20;3:e02203
pubmed: 24844245

Auteurs

Sunbin Deng (S)

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Howard Hughes Medical Institute, Boston, MA, USA.

Jiaxi Cai (J)

Department of Bioengineering, Jacobs School of Engineering, UCSD, San Diego, CA, USA.

Stephen C Harrison (SC)

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Howard Hughes Medical Institute, Boston, MA, USA.

Huilin Zhou (H)

Department of Bioengineering, Jacobs School of Engineering, UCSD, San Diego, CA, USA.
Department of Cellular and Molecular Medicine, School of Medicine, Moores Cancer Center, UCSD, San Diego, CA, USA.

Stephen M Hinshaw (SM)

Stanford Cancer Institute, Stanford School of Medicine, Stanford, CA, USA.

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Classifications MeSH