Structural basis of Stu2 recruitment to yeast kinetochores.


Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
16 02 2021
Historique:
received: 02 12 2020
accepted: 15 02 2021
pubmed: 17 2 2021
medline: 22 1 2022
entrez: 16 2 2021
Statut: epublish

Résumé

Chromosome segregation during cell division requires engagement of kinetochores of sister chromatids with microtubules emanating from opposite poles. As the corresponding microtubules shorten, these 'bioriented' sister kinetochores experience tension-dependent stabilization of microtubule attachments. The yeast XMAP215 family member and microtubule polymerase, Stu2, associates with kinetochores and contributes to tension-dependent stabilization in vitro. We show here that a C-terminal segment of Stu2 binds the four-way junction of the Ndc80 complex (Ndc80c) and that residues conserved both in yeast Stu2 orthologs and in their metazoan counterparts make specific contacts with Ndc80 and Spc24. Mutations that perturb this interaction prevent association of Stu2 with kinetochores, impair cell viability, produce biorientation defects, and delay cell cycle progression. Ectopic tethering of the mutant Stu2 species to the Ndc80c junction restores wild-type function in vivo. These findings show that the role of Stu2 in tension-sensing depends on its association with kinetochores by binding with Ndc80c.

Identifiants

pubmed: 33591274
doi: 10.7554/eLife.65389
pii: 65389
pmc: PMC7909949
doi:
pii:

Substances chimiques

Microtubule-Associated Proteins 0
NDC80 protein, S cerevisiae 0
Nuclear Proteins 0
STU2 protein, S cerevisiae 0
Saccharomyces cerevisiae Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : P30 GM124165
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007464
Pays : United States

Informations de copyright

© 2021, Zahm et al.

Déclaration de conflit d'intérêts

JZ, MS, JC, SH, MM No competing interests declared

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Auteurs

Jacob A Zahm (JA)

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

Michael G Stewart (MG)

Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.

Joseph S Carrier (JS)

Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.

Stephen C Harrison (SC)

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

Matthew P Miller (MP)

Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.

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Classifications MeSH