PMID- 10347188
OWN - NLM
STAT- MEDLINE
DCOM- 19990701
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 23
DP  - 1999 Jun 4
TI  - Molecular cloning and characterization of a mouse homolog of bacterial ClpX, a
      novel mammalian class II member of the Hsp100/Clp chaperone family.
PG  - 16311-9
AB  - In this paper, we present the molecular cloning and characterization of a murine 
      homolog of the Escherichia coli chaperone ClpX. Murine ClpX shares 38% amino acid
      sequence identity with the E. coli homolog and is a novel member of the
      Hsp100/Clp family of molecular chaperones. ClpX localizes to human chromosome
      15q22.2-22.3 and in mouse is expressed tissue-specifically as one transcript of
      approximately 2.9 kilobases (kb) predominantly within the liver and as two
      isoforms of approximately 2.6 and approximately 2.9 kb within the testes.
      Purified recombinant ClpX displays intrinsic ATPase activity, with a Km of
      approximately 25 microM and a Vmax of approximately 660 pmol min-1 microgram-1,
      which is active over a broad range of pH, temperature, ethanol, and salt
      parameters. Substitution of lysine 300 with alanine in the ATPase domain P-loop
      abolishes both ATP hydrolysis and binding. Recombinant ClpX can also interact
      with its putative partner protease subunit ClpP in overexpression experiments in 
      293T cells. Subcellular studies by confocal laser scanning microscopy localized
      murine ClpX green fluorescent protein fusions to the mitochondria. Deletion of
      the N-terminal mitochondrial targeting sequence abolished mitochondrial
      compartmentalization. Our results thus suggest that murine ClpX acts as a
      tissue-specific mammalian mitochondrial chaperone that may play a role in
      mitochondrial protein homeostasis.
FAU - Santagata, S
AU  - Santagata S
AD  - Mount Sinai School of Medicine, New York, New York 10029, USA.
      santas01@doc.mssm.edu
FAU - Bhattacharyya, D
AU  - Bhattacharyya D
FAU - Wang, F H
AU  - Wang FH
FAU - Singha, N
AU  - Singha N
FAU - Hodtsev, A
AU  - Hodtsev A
FAU - Spanopoulou, E
AU  - Spanopoulou E
LA  - eng
SI  - GENBANK/AF134983
GR  - 1 S10 RR0 9145-01/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
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 (Escherichia coli Proteins)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.92 (Endopeptidase Clp)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - EC 3.6.1.3 (ClpX protein, E coli)
RN  - EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
SB  - IM
MH  - ATPases Associated with Diverse Cellular Activities
MH  - Adenosine Triphosphatases/chemistry/*genetics/metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Chromosomes, Human, Pair 15
MH  - Cloning, Molecular
MH  - Endopeptidase Clp
MH  - Escherichia coli Proteins
MH  - Green Fluorescent Proteins
MH  - Humans
MH  - Kinetics
MH  - Liver/chemistry
MH  - Luminescent Proteins/genetics/metabolism
MH  - Male
MH  - Mice
MH  - Molecular Chaperones/chemistry/*genetics
MH  - Molecular Sequence Data
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Sequence Alignment
MH  - Serine Endopeptidases/metabolism
MH  - Testis/chemistry
MH  - Transfection
EDAT- 1999/05/29 00:00
MHDA- 1999/05/29 00:01
CRDT- 1999/05/29 00:00
PHST- 1999/05/29 00:00 [pubmed]
PHST- 1999/05/29 00:01 [medline]
PHST- 1999/05/29 00:00 [entrez]
AID - 10.1074/jbc.274.23.16311 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jun 4;274(23):16311-9. doi: 10.1074/jbc.274.23.16311.