Multifunctionality of the linker histones： an emerging role for protein-protein interactions  

作　　者：Steven J McBryant Xu Lu Jeffrey C Hansen 

机构地区：[1]Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA [2]Van Andel Institute, Grand Rapids, MI 49503, USA

出　　处：《Cell Research》2010年第5期519-528,共10页细胞研究（英文版）

摘　　要：Linker histones, e.g., H1, are best known for their ability to bind to nucleosomes and stabilize both nucleosome structure and condensed higher-order chromatin structures. However, over the years many investigators have reported specific interactions between linker histones and proteins involved in important cellular processes. The purpose of this review is to highlight evidence indicating an important alternative mode of action for H1, namely protein-protein interactions. We first review key aspects of the traditional view of linker histone action, including the importance of the H1 C-terminal domain. We then discuss the current state of knowledge of linker histone interactions with other proteins, and, where possible, highlight the mechanism of linker histone-mediated protein-protein interactions. Taken together, the data suggest a combinatorial role for the linker histones, functioning both as primary chromatin architectural proteins and simultaneously as recruitment hubs for proteins involved in accessing and modifying the chromatin fiber.

关 键 词：CHROMATIN linker histone higher-order structure NUCLEOSOMES 

分 类 号：Q51[生物学—生物化学] TM503.5[电气工程—电器]