You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Genetic Evidence That the Bacteriophage φ X174 Lysis Protein Inhibits Cell Wall Synthesis
Thomas G. Bernhardt, William D. Roof and Ry Young
Proceedings of the National Academy of Sciences of the United States of America
Vol. 97, No. 8 (Apr. 11, 2000), pp. 4297-4302
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/122149
Page Count: 6
You can always find the topics here!Topics: Cell walls, Alleles, Epics, Bacteriophages, Plasmids, Genetic mutation, Phenotypes, Transposons, DNA, Proteins
Were these topics helpful?See somethings inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Protein E, a 91-residue membrane protein of φ X174, causes lysis of the host in a growth-dependent manner reminiscent of cell wall antibiotics, suggesting E acts by inhibiting peptidoglycan synthesis. In a search for the cellular target of E, we previously have isolated recessive mutations in the host gene slyD (sensitivity to lysis) that block the lytic effects of E. The role of slyD, which encodes a FK506 binding protein-type peptidyl-prolyl cis-trans isomerase, is not fully understood. However, E mutants referred to as Epos (plates on slyD) lack a slyD requirement, indicating that slyD is not crucial for lysis. To identify the gene encoding the cellular target, we selected for survivors of Epos. In this study, we describe the isolation of dominant mutations in the essential host gene mraY that result in a general lysis-defective phenotype. mraY encodes translocase I, which catalyzes the formation of the first lipid-linked intermediate in cell wall biosynthesis. The isolation of these lysis-defective mutants supports a model in which translocase I is the cellular target of E and that inhibition of cell wall synthesis is the mechanism of lysis.
Proceedings of the National Academy of Sciences of the United States of America © 2000 National Academy of Sciences