Xenopus egg extracts increase dynamics of histone H1 on sperm chromatin.

ABSTRACT:

Background

Linker histone H1 has been studied in vivo and using reconstituted chromatin, but there have been few systematic studies of the effects of the cellular environment on its function. Due to the presence of many other chromatin factors and specific chaperones such as RanBP7/importin beta that regulate histone H1, linker histones likely function differently in vivo than in purified systems.

Methodology/principal findings

We have directly compared H1 binding to sperm nuclei in buffer versus Xenopus egg extract cytoplasm, and monitored the effects of adding nuclear import chaperones. In buffer, RanBP7 decondenses sperm nuclei, while H1 binds tightly to the chromatin and rescues RanBP7-mediated decondensation. H1 binding is reduced in cytoplasm, and H1 exhibits rapid FRA

SUBMITTER: Freedman BS 

PROVIDER: S-EPMC2947519 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature