PIIS0021925819373454.pdf (246.44 kB)
Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides: The N-terminal region of SurA is essential and sufficient for peptide binding
journal contribution
posted on 2023-06-10, 04:07 authored by Helen WebbHelen Webb, Lloyd W Ruddock, Rosalyn J Marchant, Kim Jonas, Peter KlappaOne of the rate-limiting steps in protein folding has been shown to be the cis-trans isomerization of proline residues, which is catalyzed by a range of peptidylprolyl cis-trans isomerases. To characterize the interaction between model peptides and the periplasmic peptidylprolyl cis-trans isomerase SurA from E. coli, we employed a chemical cross-linking strategy that has been used previously to elucidate the interaction of substrates with other folding catalysts. The interaction between purified SurA and model peptides was significant in that it showed saturation and was abolished by denaturation of SurA; however the interaction was independent of the presence of proline residues in the model peptides. From results obtained by limited proteolysis we conclude that an N-terminal fragment of SurA, comprising 150 amino acids that do not contain the active sites involved in the peptidylprolyl cis-trans isomerization, is essential for the binding of peptides by SurA. This was confirmed by probing the interaction of the model peptide with the recombinant N-terminal fragment, expressed in Escherichia coli. Hence we propose that, similar to protein disulfide isomerase and other folding catalysts, SurA exhibits a modular architecture composed of a substrate binding domain and distinct catalytically active domains.
History
Publication status
- Published
File Version
- Published version
Journal
Journal of Biological ChemistryISSN
0021-9258Publisher
Elsevier BVExternal DOI
Volume
276Page range
45622-45627Event location
United StatesDepartment affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2022-07-01First Open Access (FOA) Date
2022-07-01First Compliant Deposit (FCD) Date
2022-07-01Usage metrics
Categories
No categories selectedKeywords
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC