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The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity

Title data

Behrens, Susanne ; Maier, Raimund ; de Cock, Hans ; Schmid, Franz X. ; Gross, Carol A.:
The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.
In: The EMBO Journal. Vol. 20 (15 January 2001) Issue 1-2 . - pp. 285-294.
ISSN 0261-4189
DOI: https://doi.org/10.1093/emboj/20.1.285

Abstract in another language

The Escherichia coli periplasmic peptidyl-prolyl isomerase (PPIase) SurA is involved in the maturation of outer membrane porins. SurA consists of a substantial N-terminal region, two iterative parvulin-like domains and a C-terminal tail. Here we show that a variant of SurA lacking both parvulin-like domains exhibits a PPIase-independent chaperone-like activity in vitro and almost completely complements the in vivo function of intact SurA. SurA interacts preferentially (>50-fold) with in vitro synthesized porins over other similarly sized proteins, leading us to suggest that the chaperone-like function of SurA preferentially facilitates maturation of outer membrane proteins.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 9029143
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: 28 May 2015 07:20
Last Modified: 28 May 2015 07:20
URI: https://eref.uni-bayreuth.de/id/eprint/14380