THE ESCHERICHIA-COLI HFLA LOCUS ENCODES A PUTATIVE GTP-BINDING PROTEIN AND 2 MEMBRANE-PROTEINS, ONE OF WHICH CONTAINS A PROTEASE-LIKE DOMAIN

被引:66
作者
NOBLE, JA
INNIS, MA
KOONIN, EV
RUDD, KE
BANUETT, F
HERSKOWITZ, I
机构
[1] UNIV CALIF SAN FRANCISCO, SCH MED, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA
[2] NATL LIB MED, NATL CTR BIOTECHNOL INFORMAT, BETHESDA, MD 20894 USA
[3] CETUS CORP, EMERYVILLE, CA 94608 USA
关键词
BACTERIOPHAGE-LAMBDA; PROTEOLYSIS; CII-PROTEIN; LYSIS LYSOGENY DECISION;
D O I
10.1073/pnas.90.22.10866
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The hflA (high frequency of lysogenization) locus of Escherichia coli governs the lysis-lysogeny decision of bacteriophage lambda by controlling stability of the phage cII protein. hflA contains three genes, hflX, hflK, and hflC, encoding polypeptides of 50, 46, and 37 kDa, respectively. We have determined the nucleotide sequence of 3843 base pairs containing hflA and have found three large open reading frames corresponding to hflX, hflK, and hflC. HflX contains the three sequence motifs typical of GTP-binding proteins and appears to be a member of a distinct family of putative GTPases. HflC and HflK appear to be integral membrane proteins which show some similarity to each other and to a human membrane protein. The C-terminal region of HflC contains a domain resembling the catalytic domain of ClpP, a bacterial ATP-dependent protease. We hypothesize that HflK and HflC constitute a distinct membrane-bound protease whose activity may be modulated by HflX GTPase.
引用
收藏
页码:10866 / 10870
页数:5
相关论文
共 41 条
[11]   GENETIC AND PHYSIOLOGICAL RELATIONSHIPS AMONG THE MIAA GENE, 2-METHYLTHIO-N6-(DELTA-2-ISOPENTENYL)-ADENOSINE TRANSFER-RNA MODIFICATION, AND SPONTANEOUS MUTAGENESIS IN ESCHERICHIA-COLI K-12 [J].
CONNOLLY, DM ;
WINKLER, ME .
JOURNAL OF BACTERIOLOGY, 1989, 171 (06) :3233-3246
[12]  
DEFERNANDEZ MT, 1968, NATURE, V219, P585
[13]   GTP-BINDING DOMAIN - 3 CONSENSUS SEQUENCE ELEMENTS WITH DISTINCT SPACING [J].
DEVER, TE ;
GLYNIAS, MJ ;
MERRICK, WC .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (07) :1814-1818
[15]   ANALYSIS OF MEMBRANE AND SURFACE PROTEIN SEQUENCES WITH THE HYDROPHOBIC MOMENT PLOT [J].
EISENBERG, D ;
SCHWARZ, E ;
KOMAROMY, M ;
WALL, R .
JOURNAL OF MOLECULAR BIOLOGY, 1984, 179 (01) :125-142
[16]  
GAUTSCH JW, 1974, GENETICS, V77, P435
[17]   AN NTP-BINDING MOTIF IS THE MOST CONSERVED SEQUENCE IN A HIGHLY DIVERGED MONOPHYLETIC GROUP OF PROTEINS INVOLVED IN POSITIVE STRAND RNA VIRAL REPLICATION [J].
GORBALENYA, AE ;
BLINOV, VM ;
DONCHENKO, AP ;
KOONIN, EV .
JOURNAL OF MOLECULAR EVOLUTION, 1989, 28 (03) :256-268
[18]   REGULATION BY PROTEOLYSIS - ENERGY-DEPENDENT PROTEASES AND THEIR TARGETS [J].
GOTTESMAN, S ;
MAURIZI, MR .
MICROBIOLOGICAL REVIEWS, 1992, 56 (04) :592-621
[19]   CELL-GROWTH AND LAMBDA-PHAGE DEVELOPMENT CONTROLLED BY THE SAME ESSENTIAL ESCHERICHIA-COLI GENE, FTSH HFLB [J].
HERMAN, C ;
OGURA, T ;
TOMOYASU, T ;
HIRAGA, S ;
AKIYAMA, Y ;
ITO, K ;
THOMAS, R ;
DARI, R ;
BOULOC, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (22) :10861-10865
[20]   THE LYSIS-LYSOGENY DECISION OF PHAGE-LAMBDA - EXPLICIT PROGRAMMING AND RESPONSIVENESS [J].
HERSKOWITZ, I ;
HAGEN, D .
ANNUAL REVIEW OF GENETICS, 1980, 14 :399-445