Unknown

Dataset Information

0

Towards a mechanism for histone chaperones.


ABSTRACT: Histone chaperones can be broadly defined as histone-binding proteins that influence chromatin dynamics in an ATP-independent manner. Their existence reflects the importance of chromatin homeostasis and the unique and unusual biochemistry of the histone proteins. Histone supply and demand at chromatin is regulated by a network of structurally and functionally diverse histone chaperones. At the core of this network is a mechanistic variability that is only beginning to be appreciated. In this review, we highlight the challenges in determining histone chaperone mechanism and discuss possible mechanisms in the context of nucleosome thermodynamics. We discuss how histone chaperones prevent promiscuous histone interactions, and consider if this activity represents the full extent of histone chaperone function in governing chromatin dynamics. This article is part of a Special Issue entitled: Histone chaperones and Chromatin assembly.

SUBMITTER: Elsasser SJ 

PROVIDER: S-EPMC3315836 | biostudies-literature | 2013 Mar-Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Towards a mechanism for histone chaperones.

Elsässer Simon J SJ   D'Arcy Sheena S  

Biochimica et biophysica acta 20130301 3-4


Histone chaperones can be broadly defined as histone-binding proteins that influence chromatin dynamics in an ATP-independent manner. Their existence reflects the importance of chromatin homeostasis and the unique and unusual biochemistry of the histone proteins. Histone supply and demand at chromatin is regulated by a network of structurally and functionally diverse histone chaperones. At the core of this network is a mechanistic variability that is only beginning to be appreciated. In this rev  ...[more]

Similar Datasets

| S-EPMC5446181 | biostudies-literature
| S-EPMC7914515 | biostudies-literature
| S-EPMC3494481 | biostudies-literature
| S-EPMC2063486 | biostudies-literature
| S-EPMC4004086 | biostudies-literature
| S-EPMC3184832 | biostudies-literature
| S-EPMC10982699 | biostudies-literature
| S-EPMC4415165 | biostudies-literature
| S-EPMC4004355 | biostudies-literature
| S-EPMC3664809 | biostudies-other