Gene product 0.4 increases bacteriophage T7 competitiveness by inhibiting host cell division.
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Bacteriophages take over host resources primarily via the activity of proteins expressed early in infection. One of these proteins, produced by the Escherichia coli phage T7, is gene product (Gp) 0.4. Here, we show that Gp0.4 is a direct inhibitor of the E. coli filamenting temperature-sensitive mutant Z division protein. A chemically synthesized Gp0.4 binds to purified filamenting temperature-sensitive mutant Z protein and directly inhibits its assembly in vitro. Consequently, expression of Gp0.4 in vivo is lethal to E. coli and results in bacteria that are morphologically elongated. We further show that this inhibition of cell division by Gp0.4 enhances the bacteriophage's competitive ability. This division inhibition is thus a fascinating example of a strategy in bacteriophages to maximize utilization of their hosts' cell resources.
Published Version (Please cite this version)10.1073/pnas.1314096110
Publication InfoErickson, Harold Paul; Kiro, Ruth; Milam, Sara L; Molshanski-Mor, Shahar; Qimron, Udi; & Yosef, Ido (2013). Gene product 0.4 increases bacteriophage T7 competitiveness by inhibiting host cell division. Proceedings of the National Academy of Sciences of the United States of America, 110(48). 10.1073/pnas.1314096110. Retrieved from https://hdl.handle.net/10161/16465.
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James B. Duke Professor of Cell Biology
Cytoskeleton: It is now clear that the actin and microtubule cytoskeleton originated in bacteria. Our major research is on FtsZ, the bacterial tubulin homolog, which assembles into a contractile ring that divides the bacterium. We have studied FtsZ assembly in vitro, and found that it assembles into thin protofilaments (pfs). Dozens of these pfs are further clustered to form the contractile Z-ring in vivo. Some important discoveries in the last ten years include: &bul