Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0192572
Title: CENP-C/H/I/K/M/T/W/N/L and hMis12 but not CENP-S/X participate in complex formation in the nucleoplasm of living human interphase cells outside centromeres
Authors: Hoischen C.
Yavas S.
Wohland T. 
Diekmann S.
Keywords: binding protein
centromere protein C
centromere protein H
centromere protein I
centromere protein K
centromere protein L
centromere protein M
centromere protein N
centromere protein O
centromere protein P
centromere protein Q
centromere protein R
centromere protein S
centromere protein T
centromere protein U
centromere protein W
centromere protein X
Dsn1 protein
heterodimer
Mis12 protein
Nnf1 protein
Nsl1 protein
nuclear protein
unclassified drug
APITD1 protein, human
apoptosis regulatory protein
cell cycle protein
CENPH protein, human
CENPI protein, human
CENPK protein, human
CENPL protein, human
CENPN protein, human
CENPW protein, human
centromere protein C
DNA binding protein
microtubule associated protein
MIS12 protein, human
nonhistone protein
nuclear protein
proliferation associated nuclear element protein 1, human
STRA13 protein, human
tumor protein
tumor suppressor protein
amino terminal sequence
apparent dissociation constant
Article
binding site
carboxy terminal sequence
cell component
cell nucleus
cellular distribution
centromere
complex formation
controlled study
DNA binding
embryo
fluorescence correlation spectroscopy
human
human cell
kinetochore
nucleoplasm
protein aggregation
protein expression
protein localization
protein protein interaction
genetics
interphase
metabolism
neoplasm
pathology
tumor cell line
Apoptosis Regulatory Proteins
Cell Cycle Proteins
Cell Line, Tumor
Centromere
Chromosomal Proteins, Non-Histone
DNA-Binding Proteins
Humans
Interphase
Microtubule-Associated Proteins
Neoplasm Proteins
Neoplasms
Nuclear Proteins
Tumor Suppressor Proteins
Issue Date: 2018
Publisher: Public Library of Science
Citation: Hoischen C., Yavas S., Wohland T., Diekmann S. (2018). CENP-C/H/I/K/M/T/W/N/L and hMis12 but not CENP-S/X participate in complex formation in the nucleoplasm of living human interphase cells outside centromeres. PLoS ONE 13 (3) : e0192572. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0192572
Abstract: Kinetochore proteins assemble onto centromeric chromatin and regulate DNA segregation during cell division. The inner kinetochore proteins bind centromeres while most outer kinetochore proteins assemble at centromeres during mitosis, connecting the complex to microtubules. Here, we measured the co-migration between protein pairs of the constitutive centromere associated network (CCAN) and hMis12 complexes by fluorescence cross-correlation spectroscopy (FCCS) in the nucleoplasm outside centromeres in living human interphase cells. FCCS is a method that can tell if in living cells two differently fluorescently labelled molecules migrate independently, or co-migrate and thus are part of one and the same soluble complex. We also determined the apparent dissociation constants (K d ) of the hetero-dimers CENP-T/W and CENP-S/X. We measured co-migration between CENP-K and CENP-T as well as between CENP-M and CENP-T but not between CENP-T/W and CENP-S/X. Furthermore, CENP-C co-migrated with CENP-H, and CENP-K with CENP-N as well as with CENP-L. Thus, in the nucleoplasm outside centromeres, a large fraction of the CENP-H/I/K/M proteins interact with CENP-C, CENP-N/L and CENP-T/W but not with CENP-S/X. Our FCCS analysis of the Mis12 complex showed that hMis12, Nsl1, Dsn1 and Nnf1 also form a complex outside centromeres of which at least hMis12 associated with the CENP-C/H/I/K/M/T/W/N/L complex. © 2018 Hoischen et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/165911
ISSN: 19326203
DOI: 10.1371/journal.pone.0192572
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