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

Publisher: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 101229646 Publication Model: Print-Electronic Cited Medium: Print ISSN: 1742-464X (Print) Linking ISSN: 1742464X NLM ISO Abbreviation: FEBS J Subsets: MEDLINE

Original Publication: Oxford, UK : Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies, c2005-

Carrier Proteins/*metabolism ; Escherichia coli/*enzymology ; Escherichia coli Proteins/*metabolism ; Peptidylprolyl Isomerase/*metabolism; Amino Acid Motifs ; Carrier Proteins/physiology ; Cloning, Molecular ; Cross-Linking Reagents/pharmacology ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/physiology ; Models, Biological ; NIMA-Interacting Peptidylprolyl Isomerase ; Peptides/chemistry ; Peptidylprolyl Isomerase/chemistry ; Peptidylprolyl Isomerase/physiology ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Substrate Specificity

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.

United Kingdom Biotechnology and Biological Sciences Research Council

0 (Carrier Proteins)
0 (Cross-Linking Reagents)
0 (Escherichia coli Proteins)
0 (NIMA-Interacting Peptidylprolyl Isomerase)
0 (Peptides)
0 (Recombinant Proteins)
EC 5.2.1.- (PpiD protein, E coli)
EC 5.2.1.- (SurA protein, E coli)
EC 5.2.1.8 (Peptidylprolyl Isomerase)
EC 5.2.1.8 (parvA protein, E coli)

Date Created: 20080524 Date Completed: 20080731 Latest Revision: 20161124

20250114

10.1111/j.1742-4658.2008.06493.x

18498364