THE ARGININE REPRESSOR OF ESCHERICHIA-COLI

被引:132
作者
MAAS, WK
机构
关键词
D O I
10.1128/MMBR.58.4.631-640.1994
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
This review tells the story of the arginine repressor of Escherichia coli from the time of its discovery in the 1950s until the present. It describes how the research progressed through physiological, genetic, and biochemical phases and how the nature of the repressor and its interaction with its target sites were unraveled. The studies of the repression of arginine biosynthesis revealed unique features at every level of the investigations. In the early phase of the work they showed that the genes controlled by the arginine repressor were scattered over the linkage map and were not united, as in other cases, in a single operon. This led to the concept of the regulon as a physiological unit of regulation. It was also shown that different alleles of the arginine repressor could result in either inhibition of enzyme formation as in E. coli K-12, or in stimulation of enzyme formation, as in E. coli B. Later it was shown that the arginine repressor is a hexamer, whereas other repressors of biosynthetic pathways are dimers. As a consequence the arginine repressor binds to two palindromic sites rather than to one. It was found that the arginine repressor not only acts in the repression of enzyme synthesis but also is required for die resolution of plasmid multimers to monomers, a completely unrelated function. Finally, the arginine repressor does not possess characteristic structural features seen in other prokaryotic repressors, such as a helix-turn-helix motif or an antiparallel beta-sheet motif The unique features have sustained continuous interest in the arginine repressor and have mane it a challenging subject of investigation.
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页码:631 / 640
页数:10
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共 74 条
[1]   THE EVOLUTIONARY SELECTION OF DNA-BASE PAIRS IN GENE-REGULATORY BINDING-SITES [J].
BERG, OG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (16) :7501-7505
[2]   CRYSTALLIZATION OF THE ARGININE-DEPENDENT REPRESSOR ACTIVATOR AHRC FROM BACILLUS-SUBTILIS [J].
BOYS, CWG ;
CZAPLEWSKI, LG ;
PHILLIPS, SEV ;
BAUMBERG, S ;
STOCKLEY, PG .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 213 (02) :227-228
[3]   MUTANT ESCHERICHIA-COLI ARGININE REPRESSOR PROTEINS THAT FAIL TO BIND L-ARGININE, YET RETAIN THE ABILITY TO BIND THEIR NORMAL DNA-BINDING SITES [J].
BURKE, M ;
MERICAN, AF ;
SHERRATT, DJ .
MOLECULAR MICROBIOLOGY, 1994, 13 (04) :609-618
[4]   ROCR, A NOVEL REGULATORY PROTEIN CONTROLLING ARGININE UTILIZATION IN BACILLUS-SUBTILIS, BELONGS TO THE NTRC/NIFA FAMILY OF TRANSCRIPTIONAL ACTIVATORS [J].
CALOGERO, S ;
GARDAN, R ;
GLASER, P ;
SCHWEIZER, J ;
RAPOPORT, G ;
DEBARBOUILLE, M .
JOURNAL OF BACTERIOLOGY, 1994, 176 (05) :1234-1241
[5]  
CELIS TF, 1972, J MOL BIOL, V62, P179
[6]   EFFECT OF IAC REPRESSOR OLIGOMERIZATION ON REGULATORY OUTCOME [J].
CHAKERIAN, AE ;
MATTHEWS, KS .
MOLECULAR MICROBIOLOGY, 1992, 6 (08) :963-968
[7]   ARGININE REGULON OF ESCHERICHIA-COLI K-12 - A STUDY OF REPRESSOR OPERATOR INTERACTIONS AND OF INVITRO BINDING AFFINITIES VERSUS INVIVO REPRESSION [J].
CHARLIER, D ;
ROOVERS, M ;
VANVLIET, F ;
BOYEN, A ;
CUNIN, R ;
NAKAMURA, Y ;
GLANSDORFF, N ;
PIERARD, A .
JOURNAL OF MOLECULAR BIOLOGY, 1992, 226 (02) :367-386
[8]   PARAMETERS OF GENE-EXPRESSION IN BIPOLAR ARGECBH OPERON OF ESCHERICHIA-COLI-K12 - QUESTION OF TRANSLATIONAL CONTROL [J].
CUNIN, R ;
BOYEN, A ;
POUWELS, P ;
GLANSDORFF, N ;
CRABEEL, M .
MOLECULAR & GENERAL GENETICS, 1975, 140 (01) :51-60
[9]   MOLECULAR-BASIS FOR MODULATED REGULATION OF GENE-EXPRESSION IN THE ARGININE REGULON OF ESCHERICHIA-COLI K-12 [J].
CUNIN, R ;
ECKHARDT, T ;
PIETTE, J ;
BOYEN, A ;
PIERARD, A ;
GLANSDORFF, N .
NUCLEIC ACIDS RESEARCH, 1983, 11 (15) :5007-5019
[10]   INVOLVEMENT OF ARGININE IN INVITRO REPRESSION OF TRANSCRIPTION OF ARGININE GENES C, B AND H IN ESCHERICHIA-COLI-K12 [J].
CUNIN, R ;
KELKER, N ;
BOYEN, A ;
YANG, HL ;
ZUBAY, G ;
GLANSDORFF, N ;
MAAS, WK .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1976, 69 (02) :377-382