dc.contributor.author | Subramanian, L | en_US |
dc.contributor.author | Medina-Pritchard, B | en_US |
dc.contributor.author | Barton, R | en_US |
dc.contributor.author | Spiller, F | en_US |
dc.contributor.author | Kulasegaran-Shylini, R | en_US |
dc.contributor.author | Radaviciute, G | en_US |
dc.contributor.author | Allshire, RC | en_US |
dc.contributor.author | Arockia Jeyaprakash, A | en_US |
dc.date.accessioned | 2017-03-24T14:47:08Z | |
dc.date.available | 2016-02-03 | en_US |
dc.date.issued | 2016-04 | en_US |
dc.date.submitted | 2017-03-01T08:35:17.643Z | |
dc.identifier.uri | http://qmro.qmul.ac.uk/xmlui/handle/123456789/22218 | |
dc.description.abstract | Mis18 is a key regulator responsible for the centromere localization of the CENP-A chaperone Scm3 in Schizosaccharomyces pombe and HJURP in humans, which establishes CENP-A chromatin that defines centromeres. The molecular and structural determinants of Mis18 centromere targeting remain elusive. Here, by combining structural, biochemical, and yeast genetic studies, we show that the oligomerization of S. pombe Mis18, mediated via its conserved N-terminal Yippee-like domain, is crucial for its centromere localization and function. The crystal structure of the N-terminal Yippee-like domain reveals a fold containing a cradle-shaped pocket that is implicated in protein/nucleic acid binding, which we show is required for Mis18 function. While the N-terminal Yippee-like domain forms a homodimer in vitro and in vivo, full-length Mis18, including the C-terminal α-helical domain, forms a homotetramer in vitro We also show that the Yippee-like domains of human Mis18α/Mis18β interact to form a heterodimer, implying a conserved structural theme for Mis18 regulation. | en_US |
dc.description.sponsorship | Wellcome Trust Career Development Grant095822
Principal Research Fellowship095021065061
Wellcome Trust Centre Core Grant092076091020
Wellcome Trust‐University of Edinburgh Institutional Strategic Support Fund
EpiGeneSys Network of ExcellenceHEALTH‐F4‐2010‐257082
EC FP7 Marie Curie International Incoming FellowshipPIIF‐GA‐2010‐275280
EMBO Long Term FellowshipALTF 1491‐2010
Wellcome Trust | en_US |
dc.format.extent | 496 - 507 | en_US |
dc.language | eng | en_US |
dc.relation.ispartof | EMBO Rep | en_US |
dc.rights | This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. | |
dc.subject | CENP‐A | en_US |
dc.subject | Mis18 | en_US |
dc.subject | Yippee | en_US |
dc.subject | centromere | en_US |
dc.subject | epigenetics | en_US |
dc.subject | Carrier Proteins | en_US |
dc.subject | Centromere | en_US |
dc.subject | Chromosomal Proteins, Non-Histone | en_US |
dc.subject | Crystallography, X-Ray | en_US |
dc.subject | DNA-Binding Proteins | en_US |
dc.subject | Epigenesis, Genetic | en_US |
dc.subject | Molecular Chaperones | en_US |
dc.subject | Protein Domains | en_US |
dc.subject | Protein Multimerization | en_US |
dc.subject | Schizosaccharomyces | en_US |
dc.subject | Schizosaccharomyces pombe Proteins | en_US |
dc.title | Centromere localization and function of Mis18 requires Yippee-like domain-mediated oligomerization. | en_US |
dc.type | Article | |
dc.rights.holder | © 2016 The Authors | |
dc.identifier.doi | 10.15252/embr.201541520 | en_US |
pubs.author-url | https://www.ncbi.nlm.nih.gov/pubmed/26921242 | en_US |
pubs.issue | 4 | en_US |
pubs.notes | Not known | en_US |
pubs.publication-status | Published | en_US |
pubs.volume | 17 | en_US |
dcterms.dateAccepted | 2016-02-03 | en_US |