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Originally published In Press as doi:10.1074/jbc.M011699200 on January 25, 2001
J. Biol. Chem., Vol. 276, Issue 17, 13695-13700, April 27, 2001
Revisiting the Lysogenization Control of Bacteriophage
IDENTIFICATION AND CHARACTERIZATION OF A NEW HOST COMPONENT,
HflD*
Akio
Kihara ,
Yoshinori
Akiyama, and
Koreaki
Ito§
From the Institute for Virus Research, Kyoto University, Sakyo-ku,
Kyoto 606-8507, Japan
Upon infection to the Escherichia
coli cell, the genome of bacteriophage either replicates to
form new progenies (lytic growth) or integrates into the host
chromosome (lysogenization). The CII protein is a key determinant
in the lysis-lysogeny decision. It is a short-lived transcription
activator for the genes essential for lysogeny establishment. In
this study, we isolated a new class of hfl (high frequency
lysogenization) mutants of E. coli, using a new selection
for enhancement of CII-stimulated transcription. The gene affected was
termed hflD, which encodes a protein of 213 amino acids. An
hflD-disrupted mutant indeed showed an Hfl phenotype,
indicating that HflD acts to down-regulate lysogenization. HflD is
associated peripherally with the cytoplasmic membrane. Its interaction
with CII was demonstrated in vitro using purified proteins
as well as in vivo using the bacterial two-hybrid system. Pulse-chase examinations demonstrated that the HflD function is required for the rapid in vivo degradation of CII, although
it interfered with FtsH-mediated CII proteolysis in an in
vitro reaction system using detergent-solubilized components. We
suggest that HflD is a factor that sequesters CII from the target
promoters and recruits it to the membrane where the FtsH
protease is localized.
*
This work was supported by grants from CREST (Core
Research for Evolutional Science and Technology), Japan Science and
Technology Corporation (JST), and the Ministry of Education, Science
and Culture, Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a Japan Society for the Promotion of Science (JSPS)
Research Fellowship for Young Scientists. Present address: Dept. of
Cell Biology, National Inst. for Basic Biology, Nishigounaka 38, Myoudaiji-cho, Okazaki 444-8585, Japan.
§
To whom correspondence should be addressed. Fax: +81-75-771-5699;
E-mail: kito@virus.kyoto-u.ac.jp.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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