Structural characterization of KKT4, an unconventional microtubule-binding kinetochore protein.

BRCT domain KKT4 NMR spectroscopy Trypanosoma brucei X-ray crystallography coiled coil crosslinking mass spectrometry kinetochore kinetoplastid microtubules

Journal

Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697

Informations de publication

Date de publication:
02 09 2021
Historique:
received: 21 10 2020
revised: 17 02 2021
accepted: 08 04 2021
pubmed: 30 4 2021
medline: 17 3 2022
entrez: 29 4 2021
Statut: ppublish

Résumé

The kinetochore is the macromolecular machinery that drives chromosome segregation by interacting with spindle microtubules. Kinetoplastids (such as Trypanosoma brucei), a group of evolutionarily divergent eukaryotes, have a unique set of kinetochore proteins that lack any significant homology to canonical kinetochore components. To date, KKT4 is the only kinetoplastid kinetochore protein that is known to bind microtubules. Here we use X-ray crystallography, NMR spectroscopy, and crosslinking mass spectrometry to characterize the structure and dynamics of KKT4. We show that its microtubule-binding domain consists of a coiled-coil structure followed by a positively charged disordered tail. The structure of the C-terminal BRCT domain of KKT4 reveals that it is likely a phosphorylation-dependent protein-protein interaction domain. The BRCT domain interacts with the N-terminal region of the KKT4 microtubule-binding domain and with a phosphopeptide derived from KKT8. Taken together, these results provide structural insights into the unconventional kinetoplastid kinetochore protein KKT4.

Identifiants

pubmed: 33915106
pii: S0969-2126(21)00120-9
doi: 10.1016/j.str.2021.04.004
pmc: PMC8443799
pii:
doi:

Substances chimiques

Microtubule-Associated Proteins 0
Protozoan Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1014-1028.e8

Subventions

Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 210622/Z/18/Z
Pays : United Kingdom

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Ltd.. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Patryk Ludzia (P)

Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.

Edward D Lowe (ED)

Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.

Gabriele Marcianò (G)

Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.

Shabaz Mohammed (S)

Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.

Christina Redfield (C)

Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK. Electronic address: christina.redfield@bioch.ox.ac.uk.

Bungo Akiyoshi (B)

Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK. Electronic address: bungo.akiyoshi@bioch.ox.ac.uk.

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Classifications MeSH