Two arginine repressors regulate arginine biosynthesis in Lactobacillus plantarum.
The repression of the carAB operon encoding carbamoyl phosphate synthase leads to Lactobacillus plantarum FB331 growth inhibition in the presence of arginine. This phenotype was used in a positive screening to select spontaneous mutants deregulated in the arginine biosynthesis pathway. Fourteen mutants were genetically characterized for constitutive arginine production. Mutations were located either in one of the arginine repressor genes (argR1 or argR2) present in L. plantarum or in a putative ARG operator in the intergenic region of the bipolar carAB-argCJBDF operons involved in arginine biosynthesis. Although the presence of two ArgR regulators is commonly found in gram-positive bacteria, only single arginine repressors have so far been well studied in Escherichia coli or Bacillus subtilis. In L. plantarum, arginine repression was abolished when ArgR1 or ArgR2 was mutated in the DNA binding domain, or in the oligomerization domain or when an A123D mutation occurred in ArgR1. A123, equivalent to the conserved residue A124 in E. coli ArgR involved in arginine binding, was different in the wild-type ArgR2. Thus, corepressor binding sites may be different in ArgR1 and ArgR2, which have only 35% identical residues. Other mutants harbored wild-type argR genes, and 20 mutants have lost their ability to grow in normal air without carbon dioxide enrichment; this revealed a link between arginine biosynthesis and a still-unknown CO2-dependent metabolic pathway. In many gram-positive bacteria, the expression and interaction of different ArgR-like proteins may imply a complex regulatory network in response to environmental stimuli.
Nicoloff
Hervé
H
Laboratoire de Dynamique, Evolution et Expression de Génomes de Microorganismes, Université Louis Pasteur/CNRS FRE 2326, 28 rue Goethe, 67083 Strasbourg, France.
Arsène-Ploetze
Florence
F
Malandain
Cédric
C
Kleerebezem
Michiel
M
Bringel
Françoise
F
D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution / Q000235:genetics / Q000502:physiology; D001120:Arginine / Q000096:biosynthesis*; D001412:Bacillus subtilis / Q000235:genetics / Q000502:physiology; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology; D001483:Base Sequence; D002245:Carbon Dioxide / Q000378:metabolism; D004252:DNA Mutational Analysis; D004269:DNA, Bacterial / Q000737:chemistry; D021901:DNA, Intergenic; D004268:DNA-Binding Proteins / Q000235:genetics / Q000502:physiology; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics / Q000502:physiology*; D005798:Genes, Bacterial; D007778:Lactobacillus / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D020125:Mutation, Missense / Q000235:genetics / Q000502:physiology; D009875:Operator Regions, Genetic; D009876:Operon; D017434:Protein Structure, Tertiary / Q000235:genetics / Q000502:physiology; D012097:Repressor Proteins / Q000235:genetics* / Q000502:physiology; D016415:Sequence Alignment
C087018:ArgR protein, Bacteria; C490177:ArgR protein, E coli; D001426:Bacterial Proteins; D004269:DNA, Bacterial; D021901:DNA, Intergenic; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D012097:Repressor Proteins; D002245:Carbon Dioxide; D001120:Arginine