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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 |
Appears in Collections: | Elements Staff Publications |
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