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Interaction of the transmembrane domain of lysis protein E from bacteriophage phi X174 with bacterial translocase MraY and peptidyi-prolyl isomerase SlyD
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Mendel, Sharon, Holbourn, Joanne M., Schouten, James A. and Bugg, Tim. (2006) Interaction of the transmembrane domain of lysis protein E from bacteriophage phi X174 with bacterial translocase MraY and peptidyi-prolyl isomerase SlyD. MICROBIOLOGY-SGM, 152 (Part 10). pp. 2959-2967. ISSN 1350-0872
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Official URL: http://dx.doi.org/10.1099/mic.0.28776-0
Abstract
The molecular target for the bacteriolytic E protein from bacteriophage phi Chi 174, 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 E-pep, 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 E-pep 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, E-pep was found to be a potent inhibitor of SlyD-catalysed peptidylprolyl isomerization (IC50 0.15 mu M), implying a strong interaction between E and SlyD. E-pep was found to inhibit E coli MraY activity when assayed in membranes (IC50 0.8 mu M); 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.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QR Microbiology |
| Journal or Publication Title: | MICROBIOLOGY-SGM |
| Publisher: | SOC GENERAL MICROBIOLOGY |
| ISSN: | 1350-0872 |
| Date: | October 2006 |
| Volume: | 152 |
| Number: | Part 10 |
| Number of Pages: | 9 |
| Page Range: | pp. 2959-2967 |
| Identification Number: | 10.1099/mic.0.28776-0 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/32928 |
Data sourced from Thomson Reuters' Web of Knowledge
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