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Mechanism of centromere recruitment of the CENP-A chaperone HJURP and its implications for centromere licensing.

Abstract：

:Nucleosomes containing the histone H3 variant CENP-A are the epigenetic mark of centromeres, the kinetochore assembly sites required for chromosome segregation. HJURP is the CENP-A chaperone, which associates with Mis18α, Mis18β, and M18BP1 to target centromeres and deposit new CENP-A. How these proteins interact to promote CENP-A deposition remains poorly understood. Here we show that two repeats in human HJURP proposed to be functionally distinct are in fact interchangeable and bind concomitantly to the 4:2:2 Mis18α:Mis18β:M18BP1 complex without dissociating it. HJURP binds CENP-A:H4 dimers, and therefore assembly of CENP-A:H4 tetramers must be performed by two Mis18αβ:M18BP1:HJURP complexes, or by the same complex in consecutive rounds. The Mis18α N-terminal tails blockade two identical HJURP-repeat binding sites near the Mis18αβ C-terminal helices. These were identified by photo-cross-linking experiments and mutated to separate Mis18 from HJURP centromere recruitment. Our results identify molecular underpinnings of eukaryotic chromosome inheritance and shed light on how centromeres license CENP-A deposition.

journal_name

Nat Commun

journal_title

Nature communications

authors

Pan D,Walstein K,Take A,Bier D,Kaiser N,Musacchio A

doi

10.1038/s41467-019-12019-6

subject

Has Abstract

pub_date

2019-09-06 00:00:00

pages

4046

issue

1

issn

2041-1723

pii

10.1038/s41467-019-12019-6

journal_volume

10

pub_type

杂志文章

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