Overexpression of Phage HK022 Nun Protein Is Toxic for Escherichia coli

Augusto Uc-Mass; Arkady Khodursky; Lewis Brown; Max E. Gottesman

doi:10.1016/j.jmb.2008.05.030

Overexpression of Phage HK022 Nun Protein Is Toxic for Escherichia coli

Augusto Uc-Mass, Arkady Khodursky, Lewis Brown, Max E. Gottesman

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

The Nun protein of coliphage HK022 excludes superinfecting λ phage. Nun recognizes and binds to the N utilization (nut) sites on phage λ 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.

Original language	English (US)
Pages (from-to)	812-819
Number of pages	8
Journal	Journal of Molecular Biology
Volume	380
Issue number	5
DOIs	https://doi.org/10.1016/j.jmb.2008.05.030
State	Published - Jul 25 2008

Bibliographical note

Funding Information:
We thank C. Yanofsky, R. Gourse, and G. Roberts for strains. We also thank R. Washburn, L. Duarte, and C. Vitiello for helpful discussions. M.E.G. was supported by National Institutes of Health (NIH) grant GM37219. A.K. was supported by NIH grant GM066098.

Keywords

E. coli stationary-phase toxicity
fis
indole
phage HK022 Nun
transcription termination

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title = "Overexpression of Phage HK022 Nun Protein Is Toxic for Escherichia coli",

abstract = "The Nun protein of coliphage HK022 excludes superinfecting λ phage. Nun recognizes and binds to the N utilization (nut) sites on phage λ 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.",

keywords = "E. coli stationary-phase toxicity, fis, indole, phage HK022 Nun, transcription termination",

author = "Augusto Uc-Mass and Arkady Khodursky and Lewis Brown and Gottesman, {Max E.}",

note = "Funding Information: We thank C. Yanofsky, R. Gourse, and G. Roberts for strains. We also thank R. Washburn, L. Duarte, and C. Vitiello for helpful discussions. M.E.G. was supported by National Institutes of Health (NIH) grant GM37219. A.K. was supported by NIH grant GM066098. ",

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AU - Brown, Lewis

AU - Gottesman, Max E.

N1 - Funding Information: We thank C. Yanofsky, R. Gourse, and G. Roberts for strains. We also thank R. Washburn, L. Duarte, and C. Vitiello for helpful discussions. M.E.G. was supported by National Institutes of Health (NIH) grant GM37219. A.K. was supported by NIH grant GM066098.

PY - 2008/7/25

Y1 - 2008/7/25

N2 - The Nun protein of coliphage HK022 excludes superinfecting λ phage. Nun recognizes and binds to the N utilization (nut) sites on phage λ 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.

AB - The Nun protein of coliphage HK022 excludes superinfecting λ phage. Nun recognizes and binds to the N utilization (nut) sites on phage λ 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.

KW - E. coli stationary-phase toxicity

KW - fis

KW - indole

KW - phage HK022 Nun

KW - transcription termination

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Overexpression of Phage HK022 Nun Protein Is Toxic for Escherichia coli

Abstract

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