HJURP binds CENP-A via a highly conserved N-terminal domain and mediates its deposition at centromeres

被引：157

作者：

Shuaib, Muhammad ^{[1
]}

Ouararhni, Khalid ^{[1
]}

Dimitrov, Stefan ^{[2
,3
]}

Hamiche, Ali ^{[1
]}

机构：

[1] Univ Strasbourg, Inst Genet & Biol Mol & Cellulaire, CNRS, INSERM, F-67404 Illkirch Graffenstaden, France

[2] Univ Grenoble 1, INSERM, F-38041 Grenoble, France

[3] Inst Albert Bonniot, U823, F-38042 Grenoble 9, France

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2010年 / 107卷 / 04期

关键词：

histone chaperone; histone variant; HISTONE FOLD DOMAIN; FISSION YEAST SCM3; CHROMATIN REQUIRES; STRUCTURAL BASIS; IN-VITRO; PROTEIN; NUCLEOSOME; DNA; H3; CORE;

D O I：

10.1073/pnas.0913709107

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The human histone H3 variant, CENP-A, replaces the conventional histone H3 in centromeric chromatin and, together with centromerespecific DNA-binding factors, directs the assembly of the kinetochore. We purified the prenucelosomal e-CENP-A complex. We found that HJURP, a member of the complex, was required for cell cycle specific targeting of CENP-A to centromeres. HJURP facilitated efficient deposition of CENP-A/H4 tetramers to naked DNA in vitro. Bacterially expressed HJURP binds at a stoichiometric ratio to the CENP-A/H4 tetramer but not to the H3/H4 tetramer. The binding occurred through a conserved HJURP short N-terminal domain, termed CBD. The novel characteristic identified in vertebrates that we named TLTY box of CBD, was essential for formation of the HJURP-CENP-A/H4 complex. Our data identified HJURP as a vertebrate CENP-A chaperone and dissected its mode of interactions with CENP-A.

引用

页码：1349 / 1354

页数：6

共 42 条

[1] Centromeres are specialized replication domains in heterochromatin [J].