PMID- 10543959
OWN - NLM
STAT- MEDLINE
DCOM- 19991119
LR  - 20131121
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 293
IP  - 3
DP  - 1999 Oct 29
TI  - An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for 
      its chaperone function.
PG  - 685-91
AB  - p23 is a co-chaperone of the heat shock protein Hsp90. p23 binds to Hsp90 in its 
      ATP-bound state and, on its own, interacts specifically with non-native proteins.
      In our attempt to correlate these functions to specific regions of p23 we have
      identified an unstructured region in p23 that maps to the C-terminal part of the 
      protein sequence. This unstructured region is dispensible for interaction of p23 
      with Hsp90, since truncated p23 can still form complexes with Hsp90. In contrast,
      however, truncation of the C-terminal 30 amino acid residues of p23 affects the
      ability of p23 to bind non-native proteins and to prevent their non-specific
      aggregation. The isolated C-terminal region itself is not able to act as a
      chaperone nor is it possible to complement truncated p23 by addition of this
      peptide. These results imply that the binding site for Hsp90 is contained in the 
      folded domain of p23 and that for efficient interaction of p23 with non-native
      proteins both the folded domain and the C-terminal unstructured region are
      required.
CI  - Copyright 1999 Academic Press.
FAU - Weikl, T
AU  - Weikl T
AD  - Technische Universitat Munchen, Garching, 83747, Germany.
FAU - Abelmann, K
AU  - Abelmann K
FAU - Buchner, J
AU  - Buchner J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (HSP90 Heat-Shock Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Peptide Fragments)
RN  - 0 (Recombinant Proteins)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 2.3.3.1 (Citrate (si)-Synthase)
RN  - EC 3.4.21.64 (Endopeptidase K)
SB  - IM
MH  - Adenosine Triphosphate/metabolism
MH  - Binding Sites
MH  - Circular Dichroism
MH  - Citrate (si)-Synthase/chemistry/metabolism
MH  - Endopeptidase K/metabolism
MH  - HSP90 Heat-Shock Proteins/*metabolism
MH  - Humans
MH  - Molecular Chaperones/*chemistry/genetics/isolation & purification/*metabolism
MH  - Molecular Weight
MH  - Peptide Fragments/chemistry/genetics/isolation & purification/metabolism
MH  - Protein Binding
MH  - Protein Denaturation
MH  - Protein Folding
MH  - Protein Structure, Secondary
MH  - Recombinant Proteins/chemistry/genetics/isolation & purification/metabolism
MH  - Sequence Deletion/genetics
MH  - Structure-Activity Relationship
EDAT- 1999/11/02 00:00
MHDA- 1999/11/02 00:01
CRDT- 1999/11/02 00:00
PHST- 1999/11/02 00:00 [pubmed]
PHST- 1999/11/02 00:01 [medline]
PHST- 1999/11/02 00:00 [entrez]
AID - 10.1006/jmbi.1999.3172 [doi]
AID - S0022-2836(99)93172-8 [pii]
PST - ppublish
SO  - J Mol Biol. 1999 Oct 29;293(3):685-91. doi: 10.1006/jmbi.1999.3172.