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Microbiology 152 (2006), 2959-2967; DOI  10.1099/mic.0.28776-0
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Microbiology 152 (2006), 2959-2967; DOI  10.1099/mic.0.28776-0
© 2006 Society for General Microbiology

Interaction of the transmembrane domain of lysis protein E from bacteriophage {phi}X174 with bacterial translocase MraY and peptidyl-prolyl isomerase SlyD

Sharon Mendel, Joanne M. Holbourn, James A. Schouten and Timothy D. H. Bugg

Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK

Correspondence
Timothy D. H. Bugg
T.D.Bugg{at}warwick.ac.uk

The molecular target for the bacteriolytic E protein from bacteriophage {phi}X174, responsible for host cell lysis, is known to be the enzyme phospho-MurNAc-pentapeptide translocase (MraY), an integral membrane protein involved in bacterial cell wall peptidoglycan biosynthesis, with an essential role being played by peptidyl-prolyl isomerase SlyD. A synthetic 37 aa peptide Epep, containing the N-terminal transmembrane {alpha}-helix of E, was found to be bacteriolytic against Bacillus licheniformis, and inhibited membrane-bound MraY. The solution conformation of Epep was found by circular dichroism (CD) spectroscopy to be 100 % {alpha}-helical. No change in the CD spectrum was observed upon addition of purified Escherichia coli SlyD, implying that SlyD does not catalyse prolyl isomerization upon E. However, Epep was found to be a potent inhibitor of SlyD-catalysed peptidyl-prolyl isomerization (IC50 0.15 µM), implying a strong interaction between E and SlyD. Epep was found to inhibit E. coli MraY activity when assayed in membranes (IC50 0.8 µM); however, no inhibition of solubilized MraY was observed, unlike nucleoside natural product inhibitor tunicamycin. These results imply that the interaction of E with MraY is not at the MraY active site, and suggest that a protein–protein interaction is formed between E and MraY at a site within the transmembrane region.

Abbreviations: CD, circular dichroism; FKBP, FK506-binding protein; MraY, phospho-MurNAc-pentapeptide translocase




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[Abstract] [Full Text] [PDF]


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