Literature DB >> 17307857

Effect of salt shock on stability of lambdaimm434 lysogens.

Paul Shkilnyj1, Gerald B Koudelka.   

Abstract

The affinities of the bacteriophage 434 repressor for its various binding sites depend on the type and/or concentration of monovalent cations. The ability of bacteriophage 434 repressor to govern the lysis-lysogeny decision depends on the DNA binding activities of the phage's cI repressor protein. We wished to determine whether changes in the intracellular ionic environment influence the lysis-lysogeny decision of the bacteriophage lambda(imm434). Our findings show that the ionic composition within bacterial cells varies with the cation concentration in the growth media. When lambda(imm434) lysogens were grown to mid-log or stationary phase and subsequently incubated in media with increasing monovalent salt concentrations, we observed a salt concentration-dependent increase in the frequency of bacteriophage spontaneous induction. We also found that the frequency of spontaneous induction varied with the type of monovalent cation in the medium. The salt-dependent increase in phage production was unaffected by a recA mutation. These findings indicate that the salt-dependent increase in phage production is not caused by activation of the SOS pathway. Instead, our evidence suggests that salt stress induces this lysogenic bacteriophage by interfering with 434 repressor-DNA interactions. We speculate that the salt-dependent increase in spontaneous induction is due to a direct effect on the repressor's affinity for DNA. Regardless of the precise mechanism, our findings demonstrate that salt stress can regulate the phage lysis-lysogeny switch.

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Year:  2007        PMID: 17307857      PMCID: PMC1855845          DOI: 10.1128/JB.01857-06

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  50 in total

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3.  Carboxyl-terminal domain dimer interface mutant 434 repressors have altered dimerization and DNA binding specificities.

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4.  Activation of recA protein: the salt-induced structural transition.

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5.  Operator sequence context influences amino acid-base-pair interactions in 434 repressor-operator complexes.

Authors:  A C Bell; G B Koudelka
Journal:  J Mol Biol       Date:  1993-12-05       Impact factor: 5.469

6.  Osmotic shock induction of capsule synthesis in Escherichia coli K-12.

Authors:  D D Sledjeski; S Gottesman
Journal:  J Bacteriol       Date:  1996-02       Impact factor: 3.490

7.  How 434 repressor discriminates between OR1 and OR3. The influence of contacted and noncontacted base pairs.

Authors:  A C Bell; G B Koudelka
Journal:  J Biol Chem       Date:  1995-01-20       Impact factor: 5.157

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10.  Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo.

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Journal:  J Mol Biol       Date:  1991-11-20       Impact factor: 5.469

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7.  DFT investigation of the vibrational properties of GC Watson-Crick and Hoogsteen base pairs in the presence of Mg²⁺, Ca²⁺, and Cu²⁺ ions.

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8.  Entry and killing of Tetrahymena thermophila by bacterially produced Shiga toxin.

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9.  Bacteriophage 434 Hex protein prevents recA-mediated repressor autocleavage.

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