PMID- 10025965
OWN - NLM
STAT- MEDLINE
DCOM- 19990311
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 443
IP  - 3
DP  - 1999 Jan 29
TI  - R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low 
      prolyl isomerase activity in both peptide and protein-folding assays.
PG  - 367-9
AB  - Previously we reported that the R73A and H144Q variants of the yeast cyclophilin 
      Cpr3 were virtually inactive in a protease-coupled peptide assay, but retained 
      activity as catalysts of a proline-limited protein folding reaction [Scholz, C. 
      et al. (1997) FEBS Lett. 414, 69-73]. A reinvestigation revealed that in fact 
      these two mutations strongly decrease the prolyl isomerase activity of Cpr3 in 
      both the peptide and the protein-folding assay. The high folding activities found 
      previously originated from a contamination of the recombinant Cpr3 proteins with 
      the Escherichia coli protein SlyD, a prolyl isomerase that co-purifies with 
      His-tagged proteins. SlyD is inactive in the peptide assay, but highly active in 
      the protein-folding assay.
FAU - Scholz, C
AU  - Scholz C
AD  - Biochemisches Laboratorium, Universitat Bayreuth, Germany.
FAU - Maier, P
AU  - Maier P
FAU - Dolinski, K
AU  - Dolinski K
FAU - Heitman, J
AU  - Heitman J
FAU - Schmid, F X
AU  - Schmid FX
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Carrier Proteins)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (SlyD protein, E coli)
RN  - 4QD397987E (Histidine)
RN  - 83HN0GTJ6D (Cyclosporine)
RN  - 94ZLA3W45F (Arginine)
RN  - EC 3.4.21.1 (Chymotrypsin)
RN  - EC 5.2.1.8 (Peptidylprolyl Isomerase)
RN  - WM0HAQ4WNM (Tacrolimus)
SB  - IM
MH  - Arginine/genetics/metabolism
MH  - Binding Sites
MH  - Carrier Proteins/isolation & purification/metabolism
MH  - Chromatography
MH  - Chymotrypsin/metabolism
MH  - Circular Dichroism
MH  - Cyclosporine/metabolism/pharmacology
MH  - *Escherichia coli Proteins
MH  - Histidine/genetics/metabolism
MH  - Humans
MH  - Kinetics
MH  - Mitochondria/*enzymology
MH  - *Mutation
MH  - Peptidylprolyl Isomerase/antagonists & inhibitors/genetics/isolation & 
      purification/*metabolism
MH  - Protein Binding
MH  - *Protein Folding
MH  - Recombinant Fusion Proteins/antagonists & inhibitors/genetics/isolation & 
      purification/metabolism
MH  - Saccharomyces cerevisiae/*enzymology
MH  - Substrate Specificity
MH  - Tacrolimus/pharmacology
EDAT- 1999/02/20 00:00
MHDA- 1999/02/20 00:01
CRDT- 1999/02/20 00:00
PHST- 1999/02/20 00:00 [pubmed]
PHST- 1999/02/20 00:01 [medline]
PHST- 1999/02/20 00:00 [entrez]
AID - S0014-5793(98)01735-9 [pii]
AID - 10.1016/s0014-5793(98)01735-9 [doi]
PST - ppublish
SO  - FEBS Lett. 1999 Jan 29;443(3):367-9. doi: 10.1016/s0014-5793(98)01735-9.