PMID- 10652318
OWN - NLM
STAT- MEDLINE
DCOM- 20000302
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 5
DP  - 2000 Feb 4
TI  - The hsp90-related protein TRAP1 is a mitochondrial protein with distinct
      functional properties.
PG  - 3305-12
AB  - The hsp90 family of molecular chaperones was expanded recently due to the cloning
      of TRAP1 and hsp75 by yeast two-hybrid screens. Careful analysis of the human
      TRAP1 and hsp75 sequences revealed that they are identical, and we have cloned a 
      similar protein from Drosophila. Immunofluorescence data show that human TRAP1 is
      localized to mitochondria. This mitochondrial localization is supported by the
      existence of mitochondrial localization sequences in the amino termini of both
      the human and Drosophila proteins. Due to the striking homology of TRAP1 to
      hsp90, we tested the ability of TRAP1 to function as an hsp90-like chaperone.
      TRAP1 did not form stable complexes with the classic hsp90 co-chaperones p23 and 
      Hop (p60). Consistent with these observations, TRAP1 had no effect on the
      hsp90-dependent reconstitution of hormone binding to the progesterone receptor in
      vitro, nor could it substitute for hsp90 to promote maturation of the receptor to
      its hormone-binding state. However, TRAP1 is sufficiently conserved with hsp90
      such that it bound ATP, and this binding was sensitive to the hsp90 inhibitor
      geldanamycin. In addition, TRAP1 exhibited ATPase activity that was inhibited by 
      both geldanamycin and radicicol. Thus, TRAP1 has functions that are distinct from
      those of hsp90.
FAU - Felts, S J
AU  - Felts SJ
AD  - Department of Biochemistry, Mayo Graduate School, Rochester, Minnesota 55905,
      USA. felts.sara@mayo.edu
FAU - Owen, B A
AU  - Owen BA
FAU - Nguyen, P
AU  - Nguyen P
FAU - Trepel, J
AU  - Trepel J
FAU - Donner, D B
AU  - Donner DB
FAU - Toft, D O
AU  - Toft DO
LA  - eng
SI  - GENBANK/AF115775
GR  - CA67891/CA/NCI NIH HHS/United States
GR  - CA73023/CA/NCI NIH HHS/United States
GR  - DK46249/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Drosophila Proteins)
RN  - 0 (HSP90 Heat-Shock Proteins)
RN  - 0 (TRAP1 protein, human)
RN  - 0 (Trap1 protein, Drosophila)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Line
MH  - Drosophila
MH  - Drosophila Proteins/analysis/genetics/*metabolism
MH  - Fluorescent Antibody Technique
MH  - HSP90 Heat-Shock Proteins/analysis/genetics/*metabolism
MH  - Humans
MH  - Mitochondria/*metabolism
MH  - Molecular Sequence Data
MH  - Sequence Alignment
EDAT- 2000/02/01 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/02/01 09:00
PHST- 2000/02/01 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/02/01 09:00 [entrez]
AID - 10.1074/jbc.275.5.3305 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Feb 4;275(5):3305-12. doi: 10.1074/jbc.275.5.3305.