Unknown

Dataset Information

0

Snf2-family proteins: chromatin remodellers for any occasion.


ABSTRACT: Chromatin facilitates the housing of eukaryotic DNA within the nucleus and restricts access to the underlying sequences. Thus, the regulation of chromatin structure provides an excellent platform for regulating processes that require information stored within genomic DNA. Snf2 proteins are a family of helicase-like proteins that direct energy derived from ATP hydrolysis into the mechanical remodelling of chromatin structure. Here, we highlight some of the recent discoveries regarding this family of proteins and show Snf2 proteins have roles in many aspects of genetic metabolism. Recent developments include new insights into the mechanism for nucleosome spacing and histone dimer exchange; together with growing evidence for the involvement of Snf2 proteins in DNA repair.

SUBMITTER: Ryan DP 

PROVIDER: S-EPMC4162295 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Snf2-family proteins: chromatin remodellers for any occasion.

Ryan Daniel P DP   Owen-Hughes Tom T  

Current opinion in chemical biology 20110820 5


Chromatin facilitates the housing of eukaryotic DNA within the nucleus and restricts access to the underlying sequences. Thus, the regulation of chromatin structure provides an excellent platform for regulating processes that require information stored within genomic DNA. Snf2 proteins are a family of helicase-like proteins that direct energy derived from ATP hydrolysis into the mechanical remodelling of chromatin structure. Here, we highlight some of the recent discoveries regarding this family  ...[more]

Similar Datasets

| S-EPMC4267348 | biostudies-literature
| S-EPMC7497338 | biostudies-literature
| S-EPMC5777669 | biostudies-literature
| S-EPMC6371444 | biostudies-literature
| S-EPMC6458923 | biostudies-literature
| S-EPMC3493121 | biostudies-literature
| S-EPMC4871117 | biostudies-literature
| S-EPMC4260354 | biostudies-literature
| S-EPMC4256374 | biostudies-literature
| S-EPMC4709239 | biostudies-literature