Specific hydrophobic residues in the 4 helix of CII are crucial for maintaining its tetrameric structure and directing the lysogenic choice
Author:
Publisher
Microbiology Society
Subject
Virology
Reference36 articles.
1. hflB, a new Escherichia coli locus regulating lysogeny and the level of bacteriophage lambda cII protein
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3. The helix-turn-helix DNA binding motif
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5. A New Look at Bacteriophage λ Genetic Networks
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1. Stochastic Cellular Fate Decision Making by Multiple Infecting Lambda Phage;PLoS ONE;2014-08-08
2. Phage λ—New Insights into Regulatory Circuits;Bacteriophages, Part A;2012
3. To Lyse or Not to Lyse: Transient-Mediated Stochastic Fate Determination in Cells Infected by Bacteriophages;PLoS Computational Biology;2011-03-10
4. Studies on Escherichia coliHflKC suggest the presence of an unidentified λ factor that influences the lysis-lysogeny switch;BMC Microbiology;2011-02-17
5. Escherichia coli HflK and HflC can individually inhibit the HflB (FtsH)-mediated proteolysis of λCII in vitro;Archives of Biochemistry and Biophysics;2010-09
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