Structure and function of nucleosome assembly proteins

被引：128

作者：

Park, Young-Jun ^{[1
]}

Luger, Karolin

机构：

[1] Colorado State Univ, Howard Hughes Med Inst, Ft Collins, CO 80523 USA

[2] Colorado State Univ, Dept Biochem & Mol Biol, Ft Collins, CO 80523 USA

来源：

BIOCHEMISTRY AND CELL BIOLOGY | 2006年 / 84卷 / 04期

关键词：

nucleosome; NAP1; SET/TAF1; histone chaperone; chromatin assembly;

D O I：

10.1139/O06-088

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Homologues of nucleosome assembly protein 1 (NAP1) have been identified in all eukaryotes. Although initially identified as histone chaperones and chromatin-assembly factors, additional functions include roles in tissue-specific transcription regulation, apoptosis, histone shuttling, and cell-cycle regulation, and extend beyond those of a simple chaperone and assembly factor. NAP1 family members share a structurally conserved fold, the NAP domain. Here we review current knowledge of the NAP family of proteins within the context of the recently determined crystal structure of the NAP1 familys first representative, NAP1 from yeast.

引用

页码：549 / 558

页数：10

共 79 条

[31]

Lankenau S, 2003, GENETICS, V163, P611

[32] Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome [J].