PMID- 10350619
OWN - NLM
STAT- MEDLINE
DCOM- 19990712
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1431
IP  - 2
DP  - 1999 May 18
TI  - Characterisation of several Hsp70 interacting proteins from mammalian organelles.
PG  - 443-50
AB  - Since both the spectrum and characteristics of in vivo substrates with affinity
      for Hsp70 members are largely unknown, we have investigated the range and type of
      mammalian organellar proteins which selectively interact with immobilised
      Escherichia coli Hsp70 (DnaK). Amongst a subset of organellar proteins
      selectively retained on DnaK, the major constituents represent unstable proteins 
      and subunits of oligomeric proteins. The interactions with DnaK were diminished
      in the presence of mt-Hsp70 and BiP, while the complexes formed with DnaK were
      dissociated in the presence of K+ and GrpE-like co-chaperones, suggesting that
      these organellar proteins constitute general Hsp70 substrates. Protein sequence
      analysis identified the major DnaK interacting constituents as the mitochondrial 
      transcription factor A, the alpha- (but not the beta-) subunit of succinyl CoA
      synthetase, mitochondrial 2,4-dienoyl CoA reductase, endoplasmic reticulum
      cyclophilin-B, peroxisomal multifunctional enzyme and a previously undescribed
      peroxisomal protein suspected to represent an isoform of 2,4-dienoyl CoA
      reductase. The selective retention of these fully synthesised proteins on Hsp70
      most likely reflects the function of this molecular chaperone in protein
      biogenesis, but additionally, could extend the known functions of Hsp70 to
      include modulating the activities of certain proteins or enzymes which are
      important in cellular homeostasis.
FAU - Naylor, D J
AU  - Naylor DJ
AD  - Department of Horticulture, Viticulture and Oenology, The University of Adelaide,
      Waite campus, PMB1, Glen Osmond, SA 5064, Australia.
      dnaylor@waite.adelaide.edu.au
FAU - Hoogenraad, N J
AU  - Hoogenraad NJ
FAU - Hoj, P B
AU  - Hoj PB
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (GrpE-like 1 mitochondrial protein, vertebrate)
RN  - 0 (Grpel1 protein, rat)
RN  - 0 (HSP70 Heat-Shock Proteins)
RN  - 0 (Heat-Shock Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Proteins)
RN  - 660YQ98I10 (Potassium Chloride)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 3.6.1.- (dnaK protein, E coli)
SB  - IM
MH  - Adenosine Triphosphate
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cattle
MH  - Chromatography, Affinity
MH  - *Escherichia coli Proteins
MH  - HSP70 Heat-Shock Proteins/*chemistry
MH  - Heat-Shock Proteins/isolation & purification
MH  - Liver/chemistry
MH  - Mitochondria/chemistry
MH  - *Molecular Chaperones
MH  - Molecular Sequence Data
MH  - Organelles/*chemistry
MH  - Potassium Chloride
MH  - Proteins/*chemistry/isolation & purification
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Swine
EDAT- 1999/06/03 00:00
MHDA- 1999/06/03 00:01
CRDT- 1999/06/03 00:00
PHST- 1999/06/03 00:00 [pubmed]
PHST- 1999/06/03 00:01 [medline]
PHST- 1999/06/03 00:00 [entrez]
AID - S0167-4838(99)00070-9 [pii]
AID - 10.1016/s0167-4838(99)00070-9 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 May 18;1431(2):443-50. doi:
      10.1016/s0167-4838(99)00070-9.