The periplasmic peptidyl prolyl cis-trans isomerases PpiD and SurA have partially overlapping substrate specificities

Stymest, Krista H. and Klappa, Peter (2008) The periplasmic peptidyl prolyl cis-trans isomerases PpiD and SurA have partially overlapping substrate specificities. FEBS Journal, 275 (13). pp. 3470-3479. ISSN 1742464X. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1111/j.1742-4658.2008.06493.x

Abstract

One of the rate-limiting steps in protein folding has been shown to be the cis-trans isomerization of proline residues, catalysed by a range of peptidyl prolyl cis-trans isomerases (PPIases). In the periplasmic space of Escherichia coli and other Gram-negative bacteria, two PPIases, SurA and PpiD, have been identified, which show high sequence similarity to the catalytic domain of the small PPIase parvulin. This observation raises a question regarding the biological significance of two apparently similar enzymes present in the same cellular compartment: do they interact with different substrates or do they catalyse different reactions? The substrate-binding motif of PpiD has not been characterized so far, and no biochemical data were available on how this folding catalyst recognizes and interacts with substrates. To characterize the interaction between model peptides and the periplasmic PPIase PpiD from E. coli, we employed a chemical crosslinking strategy that has been used previously to elucidate the interaction of substrates with SurA. We found that PpiD interacted with a range of model peptides independently of whether they contained proline residues or not. We further demonstrate here that PpiD and SurA interact with similar model peptides, and therefore must have partially overlapping substrate specificities. However, the binding motif of PpiD appears to be less specific than that of SurA, indicating that the two PPIases might interact with different substrates. We therefore propose that, although PpiD and SurA have partially overlapping substrate specificities, they fulfil different functions in the cell.

Item Type: Article
Uncontrolled keywords: peptidyl prolyl cis-trans isomerase; periplasmic space; protein folding; protein-protein interaction; substrate specificities
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Louise Dorman
Date Deposited: 18 May 2009 15:45
Last Modified: 24 Apr 2014 08:07
Resource URI: http://kar.kent.ac.uk/id/eprint/15242 (The current URI for this page, for reference purposes)
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