Revisiting the lysogenization control of bacteriophage λ -: Identification and characterization of a new host component, HflD

被引:25
作者
Kihara, A [1 ]
Akiyama, Y [1 ]
Ito, K [1 ]
机构
[1] Kyoto Univ, Inst Virus Res, Sakyo Ku, Kyoto 6068507, Japan
关键词
D O I
10.1074/jbc.M011699200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Upon infection to the Escherichia coli cell, the genome of bacteriophage Lambda either replicates to form new progenies (lytic growth) or integrates into the host chromosome (lysogenization). The lambda CII protein is a key determinant in the lysis-lysogeny decision. It is a short-lived transcription activator for the Lambda 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.
引用
收藏
页码:13695 / 13700
页数:6
相关论文
共 44 条
[31]   CIRCUIT SIMULATION OF GENETIC NETWORKS [J].
MCADAMS, HH ;
SHAPIRO, L .
SCIENCE, 1995, 269 (5224) :650-656
[32]  
Neuwald AF, 1999, GENOME RES, V9, P27
[33]   THE ESCHERICHIA-COLI HFLA LOCUS ENCODES A PUTATIVE GTP-BINDING PROTEIN AND 2 MEMBRANE-PROTEINS, ONE OF WHICH CONTAINS A PROTEASE-LIKE DOMAIN [J].
NOBLE, JA ;
INNIS, MA ;
KOONIN, EV ;
RUDD, KE ;
BANUETT, F ;
HERSKOWITZ, I .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (22) :10866-10870
[34]  
Schumann W, 1999, FEMS MICROBIOL REV, V23, P1
[35]   Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli [J].
Shotland, Y ;
Koby, S ;
Teff, D ;
Mansur, N ;
Oren, DA ;
Tatematsu, K ;
Tomoyasu, T ;
Kessel, M ;
Bukau, B ;
Ogura, T ;
Oppenheim, AB .
MOLECULAR MICROBIOLOGY, 1997, 24 (06) :1303-1310
[36]  
STAHL FW, 1986, GENETICS, V113, P215
[37]   USE OF BACTERIOPHAGE-T7 RNA-POLYMERASE TO DIRECT SELECTIVE HIGH-LEVEL EXPRESSION OF CLONED GENES [J].
STUDIER, FW ;
MOFFATT, BA .
JOURNAL OF MOLECULAR BIOLOGY, 1986, 189 (01) :113-130
[38]   DETERMINANTS OF THE QUANTITY OF THE STABLE SECY COMPLEX IN THE ESCHERICHIA-COLI CELL [J].
TAURA, T ;
BABA, T ;
AKIYAMA, Y ;
ITO, K .
JOURNAL OF BACTERIOLOGY, 1993, 175 (24) :7771-7775
[39]   MODULATION OF STABILITY OF THE ESCHERICHIA-COLI HEAT-SHOCK REGULATORY FACTOR-SIGMA-32 [J].
TILLY, K ;
SPENCE, J ;
GEORGOPOULOS, C .
JOURNAL OF BACTERIOLOGY, 1989, 171 (03) :1585-1589
[40]   TOPOLOGY AND SUBCELLULAR-LOCALIZATION OF FTSH PROTEIN IN ESCHERICHIA-COLI [J].
TOMOYASU, T ;
YAMANAKA, K ;
MURATA, K ;
SUZAKI, T ;
BOULOC, P ;
KATO, A ;
NIKI, H ;
HIRAGA, S ;
OGURA, T .
JOURNAL OF BACTERIOLOGY, 1993, 175 (05) :1352-1357