TY - JOUR
T1 - Gene product 0.4 increases bacteriophage T7 competitiveness by inhibiting host cell division
AU - Kiro, Ruth
AU - Molshanski-Mor, Shahar
AU - Yosef, Ido
AU - Milam, Sara L.
AU - Erickson, Harold P.
AU - Qimron, Udi
PY - 2013/11/26
Y1 - 2013/11/26
N2 - 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.
AB - 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.
KW - Bacterial division
KW - Bacteriophage biology
KW - Host takeover
UR - http://www.scopus.com/inward/record.url?scp=84888367816&partnerID=8YFLogxK
U2 - https://doi.org/10.1073/pnas.1314096110
DO - https://doi.org/10.1073/pnas.1314096110
M3 - Article
C2 - 24218612
SN - 0027-8424
VL - 110
SP - 19549
EP - 19554
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 48
ER -