HflD, an Escherichia coli protein involved in the λ lysis-lysogeny switch, impairs transcription activation by λCII

Pabitra K. Parua; Avisek Mondal; Pradeep Parrack

doi:10.1016/j.abb.2009.10.010

HflD, an Escherichia coli protein involved in the λ lysis-lysogeny switch, impairs transcription activation by λCII

Pabitra K. Parua, Avisek Mondal, Pradeep Parrack

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

9 Scopus citations

Abstract

The CII protein of bacteriophage lambda is the key regulator for the lytic-lysogenic choice of the viral lifecycle. An unstable homotetrameric transcription activator of the three phage promoters p_E, p_I and p_aQ, λCII is stabilized by λCIII and destabilized by the host protease, Escherichia coli HflB (FtsH). In addition, other E. coli proteins HflK, HflC and HflD also influence lysogeny by acting upon CII. Among these, HflD (22.9 kDa), a peripheral membrane protein that is exposed towards the cytoplasm, interacts with CII and decreases the frequency of lysogenization of λ by stimulating the degradation of CII. In this study, we show that in addition to helping CII degradation, HflD inhibits the DNA binding by CII, thereby inhibiting CII-dependent transcription activation. From biochemical, biophysical and modelling studies we also suggest that HflD-CII interaction takes place through the Cys31-accessible surface area of monomeric HflD, which binds to tetrameric CII as a 1:1 complex.

Original language	English (US)
Pages (from-to)	175-183
Number of pages	9
Journal	Archives of Biochemistry and Biophysics
Volume	493
Issue number	2
DOIs	https://doi.org/10.1016/j.abb.2009.10.010
State	Published - Jan 15 2010
Externally published	Yes

Keywords

λCII
Bacteriophage lambda
CII-HflD interaction
Lysis-lysogeny decision
Transcription inhibition

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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title = "HflD, an Escherichia coli protein involved in the λ lysis-lysogeny switch, impairs transcription activation by λCII",

abstract = "The CII protein of bacteriophage lambda is the key regulator for the lytic-lysogenic choice of the viral lifecycle. An unstable homotetrameric transcription activator of the three phage promoters pE, pI and paQ, λCII is stabilized by λCIII and destabilized by the host protease, Escherichia coli HflB (FtsH). In addition, other E. coli proteins HflK, HflC and HflD also influence lysogeny by acting upon CII. Among these, HflD (22.9 kDa), a peripheral membrane protein that is exposed towards the cytoplasm, interacts with CII and decreases the frequency of lysogenization of λ by stimulating the degradation of CII. In this study, we show that in addition to helping CII degradation, HflD inhibits the DNA binding by CII, thereby inhibiting CII-dependent transcription activation. From biochemical, biophysical and modelling studies we also suggest that HflD-CII interaction takes place through the Cys31-accessible surface area of monomeric HflD, which binds to tetrameric CII as a 1:1 complex.",

keywords = "λCII, Bacteriophage lambda, CII-HflD interaction, Lysis-lysogeny decision, Transcription inhibition",

author = "Parua, {Pabitra K.} and Avisek Mondal and Pradeep Parrack",

year = "2010",

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doi = "10.1016/j.abb.2009.10.010",

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T1 - HflD, an Escherichia coli protein involved in the λ lysis-lysogeny switch, impairs transcription activation by λCII

AU - Parua, Pabitra K.

AU - Mondal, Avisek

AU - Parrack, Pradeep

PY - 2010/1/15

Y1 - 2010/1/15

N2 - The CII protein of bacteriophage lambda is the key regulator for the lytic-lysogenic choice of the viral lifecycle. An unstable homotetrameric transcription activator of the three phage promoters pE, pI and paQ, λCII is stabilized by λCIII and destabilized by the host protease, Escherichia coli HflB (FtsH). In addition, other E. coli proteins HflK, HflC and HflD also influence lysogeny by acting upon CII. Among these, HflD (22.9 kDa), a peripheral membrane protein that is exposed towards the cytoplasm, interacts with CII and decreases the frequency of lysogenization of λ by stimulating the degradation of CII. In this study, we show that in addition to helping CII degradation, HflD inhibits the DNA binding by CII, thereby inhibiting CII-dependent transcription activation. From biochemical, biophysical and modelling studies we also suggest that HflD-CII interaction takes place through the Cys31-accessible surface area of monomeric HflD, which binds to tetrameric CII as a 1:1 complex.

AB - The CII protein of bacteriophage lambda is the key regulator for the lytic-lysogenic choice of the viral lifecycle. An unstable homotetrameric transcription activator of the three phage promoters pE, pI and paQ, λCII is stabilized by λCIII and destabilized by the host protease, Escherichia coli HflB (FtsH). In addition, other E. coli proteins HflK, HflC and HflD also influence lysogeny by acting upon CII. Among these, HflD (22.9 kDa), a peripheral membrane protein that is exposed towards the cytoplasm, interacts with CII and decreases the frequency of lysogenization of λ by stimulating the degradation of CII. In this study, we show that in addition to helping CII degradation, HflD inhibits the DNA binding by CII, thereby inhibiting CII-dependent transcription activation. From biochemical, biophysical and modelling studies we also suggest that HflD-CII interaction takes place through the Cys31-accessible surface area of monomeric HflD, which binds to tetrameric CII as a 1:1 complex.

KW - λCII

KW - Bacteriophage lambda

KW - CII-HflD interaction

KW - Lysis-lysogeny decision

KW - Transcription inhibition

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HflD, an Escherichia coli protein involved in the λ lysis-lysogeny switch, impairs transcription activation by λCII

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