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PMID: 2190212 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 87 ·No. 11 ·1990-06-00 ·Pages 4028-32

Liu J, Walsh CT

Abstract

The prokaryotic peptidyl-prolyl cis-trans-isomerase called "rotamase", a homolog of the human cyclophilin, has been identified in Escherichia coli. The E. coli rotamase, a product of the gene we suggest be called "rot," has been purified to homogeneity after cloning of the gene by the polymerase chain reaction and its overexpression in E. coli. Based on the chymotrypsin-coupled assay using the tetrapeptide substrate succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, the purified protein has rotamase activity identical to human cyclophilin with a catalytic efficiency close to the upper diffusional limit (kcat/Km approximately 1.0 x 10(7) M-1 x S-1 at 10 degrees C). Unlike the human cyclophilins, however, the E. coli rotamase is not significantly inhibited by the immunosuppressant drug cyclosporin A. By spheroplast fractionation of cells harboring the expression vector for the complete rot gene, the rotamase is located in the periplasm, where it could function in refolding of secreted proteins.

MeSH Terms
Amino Acid Isomerases/antagonists & inhibitors,genetics,isolation & purification,metabolism Amino Acid Sequence Bacterial Proteins/antagonists & inhibitors,genetics,isolation & purification,metabolism Base Sequence Carrier Proteins/metabolism Cloning, Molecular Cyclosporins/pharmacology Escherichia coli/enzymology,genetics,ultrastructure Genes, Bacterial Molecular Sequence Data Peptidylprolyl Isomerase Polymerase Chain Reaction Substrate Specificity
Chemicals
Bacterial Proteins Carrier Proteins Cyclosporins Amino Acid Isomerases Peptidylprolyl Isomerase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Liu J
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
Walsh C T
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.87.11.4028
Published
1990-06-00
Pages
4028-32
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC54040
Subset
IM
Grants
NIGMS NIH HHS · GM20011 · United States
External Links
PubMed source DOI: 10.1073/pnas.87.11.4028 PMC Full Text View journal details
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