A novel histone H4 arginine 3 methylation-sensitive histone H4 binding activity and transcriptional regulatory function for signal recognition particle subunits SRP68 and SRP72.

ABSTRACT:

Background

Histone methylation is believed to recruit specific histone-binding proteins.

Results

We identified SRP68/72 heterodimers as major nuclear proteins whose binding of histone H4 tail is inhibited by H4R3 methylation.

Conclusion

SRP68/72 are novel histone H4-binding proteins.

Significance

Uncovers a novel chromatin regulatory function for SRP68/72 and suggests that histone arginine methylation may function mainly in inhibiting rather than recruiting effector proteins. Arginine methylation broadly occurs in the tails of core histones. However, the mechanisms by which histone arginine methylation regulates transcription remain poorly understood. In this study we attempted to identify nuclear proteins that specifically recognize methylated arginine 3 in th

SUBMITTER: Li J 

PROVIDER: S-EPMC3504777 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature