| Literature DB >> 18571198 |
Augusto Uc-Mass1, Arkady Khodursky, Lewis Brown, Max E Gottesman.
Abstract
The Nun protein of coliphage HK022 excludes superinfecting lambda phage. Nun recognizes and binds to the N utilization (nut) sites on phage lambda nascent RNA and induces transcription termination. Overexpression of Nun from a high-copy plasmid is toxic for Escherichia coli, despite the fact that nut sites are not encoded in the E. coli genome. Cells expressing Nun cannot exit stationary phase. Toxicity is related to transcription termination, since host and nun mutations that block termination also suppress cell killing. Nun inhibits expression of wild-type lacZ, but not lacZ expressed from the Crp/cAMP-independent lacUV5 promoter. Microarray and proteomic analyses show that Nun down-regulates crp and tnaA. Crp overexpression and high indole concentrations partially reverse Nun-mediated toxicity and restore lacZ expression.Entities:
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Year: 2008 PMID: 18571198 PMCID: PMC2597491 DOI: 10.1016/j.jmb.2008.05.030
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469