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Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding

Title data

Tropschug, Maximilian ; Wachter, Elmar ; Mayer, Sabine ; Schönbrunner, Erhard Ralf ; Schmid, Franz X.:
Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding.
In: Nature. Vol. 346 (16 August 1990) Issue 6285 . - pp. 674-677.
ISSN 1476-4687
DOI: https://doi.org/10.1038/346674a0

Abstract in another language

Slow protein-folding reactions are accelerated by a prolyl cis/trans isomerase isolated from porcine kidney which is identical to cyclophilin, a protein that is probably the cellular receptor for the immunosuppressant cyclosporin A. Catalysis probably involves the isomerization of prolyl peptide bonds in the folding protein chains. Cyclosporin A inhibits folding catalysis by cyclophilin. Here we report the isolation, cloning, sequencing and expression of another protein with prolyl isomerase activity from Neurospora crassa which is unrelated to cyclophilin and which also catalyses slow steps in protein folding. This protein does, however, show sequence similarity to a human protein that binds to another, recently discovered immunosuppressive drug, FK506. Moreover, it shares 39% identity with the carboxy-terminal 114 residues of a cell-surface protein from the bacterium Legionella pneumophila, the causative agent of Legionnaires' disease. Catalysis of folding by the FK506-binding protein from N. crassa is inhibited by FK506, but not by cyclosporin A. Thus, at least two different classes of conformationally active enzymes (conformases) exist that catalyse slow steps in protein folding. Both occur in a wide variety of cells and are inhibited by immunosuppressive drugs.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 1696687
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 12 May 2015 08:25
Last Modified: 01 Jul 2016 12:02
URI: https://eref.uni-bayreuth.de/id/eprint/13296