Genes and enzymes of the acetyl cycle of arginine biosynthesis in Corynebacterium glutamicum: enzyme evolution in the early steps of the arginine pathway.
A cluster of arginine biosynthetic genes of Corynebacterium glutamicum ATCC 13032, comprising argJ, argB and argD as well as part of argC and argF, has been cloned by heterologous complementation of an Escherichia coli argE mutant. The gene order has been established as argCJBDF by sequencing the entire 4.4 kb cloned DNA fragment. The C. glutamicum argB gene can be transcribed in E. coli cells from an internal promoter located in the coding part of the preceding argJ gene, whereas transcription of the argJ gene appears vector-dependent. Expression of the corynebacterial argB gene is repressed by arginine in the native host but not in recombinant E. coli cells. Feedback inhibition of the corresponding N-acetylglutamate kinase activity was observed both in cell extracts of C. glutamicum and in recombinant E. coli argB auxotrophic strains. Extracts of E. coli cells carrying cloned corynebacterial DNA display an ornithine acetyltransferase activity (encoded by argJ) which alleviates the acetylornithinase (encoded by argE) deficiency of the enterobacterial host. In contrast to Bacillus stearothermophilus ornithine acetyltransferase which also exhibits acetylglutamate synthase activity, C. glutamicum ornithine acetyltransferase appears monofunctional. ArgA and ArgB proteins from different sources share highly significant similarities. The evolutionary implications of these data are discussed.
Sakanyan
Vehary
V
Laboratoire de Biotechnologie, Faculté des Sciences et des Techniques, Université de Nantes, 2, rue de la Houssinière, F-44072 Nantes Cedex 03, France.
Petrosyan
Pavel
P
Pharmagen, Knunyants Street 4, Yerevan 375010, Republic of Armenia.
Lecocq
Michèle
M
Laboratoire de Biotechnologie, Faculté des Sciences et des Techniques, Université de Nantes, 2, rue de la Houssinière, F-44072 Nantes Cedex 03, France.
Boyen
Anne
A
Microbiologie, Vrije Universiteit Brussel, Research Institute, CERIA-COOVI.|Microbiologie, Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut voor Biotechnologie.
Legrain
Christiane
C
Microbiologie, Vrije Universiteit Brussel, 1 avenue Emile Gryson, B-1070 Brussels, Belgium.
Demarez
Marc
M
Microbiologie, Vrije Universiteit Brussel, 1 avenue Emile Gryson, B-1070 Brussels, Belgium.
Hallet
Jean-Noël
JN
Laboratoire de Biotechnologie, Faculté des Sciences et des Techniques, Université de Nantes, 2, rue de la Houssinière, F-44072 Nantes Cedex 03, France.
Glansdorff
Nicolas
N
Microbiologie, Vrije Universiteit Brussel, 1 avenue Emile Gryson, B-1070 Brussels, Belgium.|Microbiologie, Vrije Universiteit Brussel, Research Institute, CERIA-COOVI.|Microbiologie, Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut voor Biotechnologie.
D000107:Acetylation; D000595:Amino Acid Sequence; D001120:Arginine / Q000096:biosynthesis* / Q000494:pharmacology; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics*; D001483:Base Sequence; D005075:Biological Evolution; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D003352:Corynebacterium / Q000201:enzymology / Q000235:genetics*; D004794:Enzyme Repression; D004926:Escherichia coli / Q000235:genetics; D005246:Feedback; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D017851:Phosphotransferases (Carboxyl Group Acceptor) / Q000235:genetics; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000096:biosynthesis; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D001120:Arginine; D017851:Phosphotransferases (Carboxyl Group Acceptor); C018721:acetylglutamate kinase