PMID- 22435809
OWN - NLM
STAT- MEDLINE
DCOM- 20120711
LR  - 20220321
IS  - 1470-8752 (Electronic)
IS  - 0300-5127 (Linking)
VI  - 40
IP  - 2
DP  - 2012 Apr
TI  - H1 and HMGB1: modulators of chromatin structure.
PG  - 341-6
LID - 10.1042/BST20120014 [doi]
AB  - Histone H1 and HMGB1 (high-mobility group protein B1) are the most abundant 
      chromosomal proteins apart from the core histones (on average, one copy per 
      nucleosome and per ten nucleosomes respectively). They are both highly mobile in 
      the cell nucleus, with high on/off rates for binding. In vivo and in vitro 
      evidence shows that both are able to organize chromatin structure, with H1 
      binding resulting in a more stable structure and HMGB1 binding in a less stable 
      structure. The binding sites for H1 and HMGB1 in chromatin are partially 
      overlapping, and replacement of H1 by HMGB1 through the highly dynamic nature of 
      their binding, possibly facilitated by interaction between them, could result in 
      switching of chromatin states. Binding of HMGB1 to DNA or chromatin is regulated 
      by its long and highly acidic tail, which is also involved in H1 binding. The 
      present article focuses mainly on HMGB1 and its interaction with chromatin and 
      H1, as well as its chaperone role in the binding of certain transcription factors 
      (e.g. p53) to their cognate DNA.
FAU - Thomas, Jean O
AU  - Thomas JO
AD  - Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, 
      Cambridge CB2 1GA, U.K. jot1@cam.ac.uk
FAU - Stott, Katherine
AU  - Stott K
LA  - eng
GR  - G0401547/MRC_/Medical Research Council/United Kingdom
GR  - BB/D002257/1/BB_/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
GR  - G401547/MRC_/Medical Research Council/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - Biochem Soc Trans
JT  - Biochemical Society transactions
JID - 7506897
RN  - 0 (Chromatin)
RN  - 0 (HMGB1 Protein)
RN  - 0 (Histones)
RN  - 0 (Molecular Chaperones)
SB  - IM
MH  - Animals
MH  - Chromatin/*chemistry/*metabolism
MH  - HMGB1 Protein/chemistry/*metabolism
MH  - Histones/*metabolism
MH  - Humans
MH  - Molecular Chaperones/metabolism
MH  - Protein Binding
EDAT- 2012/03/23 06:00
MHDA- 2012/07/12 06:00
CRDT- 2012/03/23 06:00
PHST- 2012/03/23 06:00 [entrez]
PHST- 2012/03/23 06:00 [pubmed]
PHST- 2012/07/12 06:00 [medline]
AID - BST20120014 [pii]
AID - 10.1042/BST20120014 [doi]
PST - ppublish
SO  - Biochem Soc Trans. 2012 Apr;40(2):341-6. doi: 10.1042/BST20120014.