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PROSITE documentation PDOC51793 [for PROSITE entry PS51793]

Mis18 domain profile





Description

The centromere is the chromosomal site that joins to microtubules during mitosis for proper segregation. Centromere protein A (CENP-A) is a histone H3 variant and an essential component of centromeres. Mis18 proteins are involved in the priming of centromeres for recruitment of CENP-A. They possess two structurally distinct domains: an N-terminal globular domain mainly comprised of β-strands and a C-terminal α-helical domain. The oligomerization of Mis18, mediated by its conserved N-terminal globular domain, is crucial for its centromere localization and function [1,2].

The Mis18 domain is mainly comprised of β-strands (see <PDB:5HJ0>) and has two conserved C-x-x-C motifs, which are signatures motifs present in metal ion-binding proteins. The overall fold of the Mis18 domain is formed by antiparallel β-sheets: a three stranded (β1-β2-β9: β-sheet I) and a six stranded (β3-β4-β8-β7-β6-β5: β-sheet II) sheet, arranged approximately perpendicular to each other. The two β-sheets are held together by a Zn(2+) ion coordinated via the C-x-x-C motifs from loops L1 and L5. The Mis18 domain contains a cradle-shaped pocket that is implicated in protein/nucleic acid binding, which is required for Mis18 function [1,2].

The profile we developed covers the entire Mis18 domain.

Last update:

April 2016 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

MIS18, PS51793; Mis18 domain profile  (MATRIX)


References

1AuthorsFujita Y. Hayashi T. Kiyomitsu T. Toyoda Y. Kokubu A. Obuse C. Yanagida M.
TitlePriming of centromere for CENP-A recruitment by human hMis18alpha, hMis18beta, and M18BP1.
SourceDev. Cell 12:17-30(2007).
PubMed ID17199038
DOI10.1016/j.devcel.2006.11.002

2AuthorsSubramanian L. Medina-Pritchard B. Barton R. Spiller F. Kulasegaran-Shylini R. Radaviciute G. Allshire R.C. Arockia Jeyaprakash A.
TitleCentromere localization and function of Mis18 requires Yippee-like domain-mediated oligomerization.
SourceEMBO Rep. 0:0-0(2016).
PubMed ID26921242
DOI10.15252/embr.201541520



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