H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain

H1 histones bind to DNA as they enter and exit the nucleosome. H1 histones have a tripartite structure consisting of a short N-terminal domain, a highly conserved central globular domain, and a lysine-and arginine-rich C-terminal domain. The C-terminal domain comprises approximately half of the tota...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 2005-07, Vol.280 (30), p.27809-27814
Main Authors: Th'ng, John P H, Sung, Rohyun, Ye, Ming, Hendzel, Michael J
Format: Article
Language:English
Subjects:
Arginine - chemistry
Cell Line, Tumor
Cell Nucleus - metabolism
Chromatin - chemistry
Cloning, Molecular
Fluorescence Recovery After Photobleaching
Fluorescence Resonance Energy Transfer
Green Fluorescent Proteins - chemistry
Histones - chemistry
Histones - metabolism
Humans
Lysine - chemistry
Microscopy, Fluorescence
Peptides - chemistry
Phosphorylation
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Time Factors
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:H1 histones bind to DNA as they enter and exit the nucleosome. H1 histones have a tripartite structure consisting of a short N-terminal domain, a highly conserved central globular domain, and a lysine-and arginine-rich C-terminal domain. The C-terminal domain comprises approximately half of the total amino acid content of the protein, is essential for the formation of compact chromatin structures, and contains the majority of the amino acid variations that define the individual histone H1 family members. This region contains several cell cycle-regulated phosphorylation sites and is thought to function through a charge-neutralization process, neutralizing the DNA phosphate backbone to allow chromatin compaction. In this study, we use fluorescence microscopy and fluorescence recovery after photobleaching to define the behavior of the individual histone H1 subtypes in vivo. We find that there are dramatic differences in the binding affinity of the individual histone H1 subtypes in vivo and differences in their preference for euchromatin and heterochromatin. Further, we show that subtype-specific properties originate with the C terminus and that the differences in histone H1 binding are not consistent with the relatively small changes in the net charge of the C-terminal domains.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M501627200