Centromere localization and function of Mis18 requires Yippee-like domain-mediated oligomerization

Jeyaprakash lab paper featured in EMBO Reports.

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Image from Jeyaprakash paper, EMBO reports 2016

Authors

Subramanian, L., Medina-Pritchard, B., Barton, R., Spiller, F., Kulasegaran-Shylini, R., Radaviciute, G., Allshire, R. C and Jeyaprakash, A. A.

Summary

This study presents the structural characterisation of Mis18, a key regulator responsible for the centromere localisation of the CENP-A specific chaperone HJURP in humans and Scm3 in S. pombe.  While the conserved N-terminal 'Yippee-like' domain possesses an intrinsic ability to dimerise, the full length S. pombe Mis18 forms a tetramer and this oligomeric structure, mediated via its 'Yippee-like' domain, is crucial for Mis18 centromere localisation and function.

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