PMID- 18241198
OWN - NLM
STAT- MEDLINE
DCOM- 20080425
LR  - 20211027
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 411
IP  - 3
DP  - 2008 May 1
TI  - A critical role in structure-specific DNA binding for the acetylatable lysine 
      residues in HMGB1.
PG  - 553-61
LID - 10.1042/BJ20071613 [doi]
AB  - The structure-specific DNA-binding protein HMGB1 (high-mobility group protein B1) 
      which comprises two tandem HMG boxes (A and B) and an acidic C-terminal tail, is 
      acetylated in vivo at Lys(2) and Lys(11) in the A box. Mutation to alanine of 
      both residues in the isolated A domain, which has a strong preference for 
      pre-bent DNA, abolishes binding to four-way junctions and 88 bp DNA minicircles. 
      The same mutations in full-length HMGB1 also abolish its binding to four-way 
      junctions, and binding to minicircles is substantially impaired. In contrast, 
      when the acidic tail is absent (AB di-domain) there is little effect of the 
      double mutation on four-way junction binding, although binding to minicircles is 
      reduced approximately 15-fold. Therefore it appears that in AB the B domain is 
      able to substitute for the non-functional A domain, whereas in full-length HMGB1 
      the B domain is masked by the acidic tail. In no case does single substitution of 
      Lys(2) or Lys(11) abolish DNA binding. The double mutation does not significantly 
      perturb the structure of the A domain. We conclude that Lys(2) and Lys(11) are 
      critical for binding of the isolated A domain and HMGB1 to distorted DNA 
      substrates.
FAU - Assenberg, Rene
AU  - Assenberg R
AD  - Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, 
      Cambridge CB2 1GA, UK.
FAU - Webb, Michelle
AU  - Webb M
FAU - Connolly, Edward
AU  - Connolly E
FAU - Stott, Katherine
AU  - Stott K
FAU - Watson, Matthew
AU  - Watson M
FAU - Hobbs, Josie
AU  - Hobbs J
FAU - Thomas, Jean O
AU  - Thomas JO
LA  - eng
GR  - BB/E013228/1/BB_/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
GR  - 8/B12904/BB_/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
GR  - WT_/Wellcome Trust/United Kingdom
GR  - BB/D002257/1/BB_/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (HMGB1 Protein)
RN  - 9007-49-2 (DNA)
RN  - EC 2.3.1.48 (CREB-Binding Protein)
RN  - K3Z4F929H6 (Lysine)
SB  - IM
MH  - Acetylation
MH  - Amino Acid Motifs
MH  - Amino Acid Sequence
MH  - CREB-Binding Protein/metabolism
MH  - Circular Dichroism
MH  - DNA/*chemistry/*metabolism
MH  - HMGB1 Protein/*chemistry/genetics/isolation & purification/*metabolism
MH  - Lysine/genetics/*metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Mutation/genetics
MH  - Nuclear Magnetic Resonance, Biomolecular
MH  - *Nucleic Acid Conformation
MH  - Protein Binding
MH  - Protein Structure, Tertiary
EDAT- 2008/02/05 09:00
MHDA- 2008/04/26 09:00
CRDT- 2008/02/05 09:00
PHST- 2008/02/05 09:00 [pubmed]
PHST- 2008/04/26 09:00 [medline]
PHST- 2008/02/05 09:00 [entrez]
AID - BJ20071613 [pii]
AID - 10.1042/BJ20071613 [doi]
PST - ppublish
SO  - Biochem J. 2008 May 1;411(3):553-61. doi: 10.1042/BJ20071613.