Journal
CELL RESEARCH
Volume 20, Issue 5, Pages 519-528Publisher
INST BIOCHEMISTRY & CELL BIOLOGY
DOI: 10.1038/cr.2010.35
Keywords
chromatin; linker histone; higher-order structure; nucleosomes
Categories
Funding
- National Institutes of Health [GM45916]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R29GM045916, R01GM045916] Funding Source: NIH RePORTER
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available