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PDBsum entry 5hj0
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References listed in PDB file
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Key reference
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Title
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Centromere localization and function of mis18 requires yippee-Like domain-Mediated oligomerization.
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Authors
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L.Subramanian,
B.Medina-Pritchard,
R.Barton,
F.Spiller,
R.Kulasegaran-Shylini,
G.Radaviciute,
R.C.Allshire,
A.Arockia jeyaprakash.
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Ref.
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Embo Rep, 2016,
17,
496-507.
[DOI no: ]
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PubMed id
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Abstract
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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.
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