GENES AND ENZYMES OF THE ACETYL CYCLE OF ARGININE-BIOSYNTHESIS IN CORYNEBACTERIUM-GLUTAMICUM - ENZYME EVOLUTION IN THE EARLY STEPS OF THE ARGININE PATHWAY
V. Sakanyan et al., GENES AND ENZYMES OF THE ACETYL CYCLE OF ARGININE-BIOSYNTHESIS IN CORYNEBACTERIUM-GLUTAMICUM - ENZYME EVOLUTION IN THE EARLY STEPS OF THE ARGININE PATHWAY, Microbiology, 142, 1996, pp. 99-108
A cluster of arginine biosynthetic genes of Corynebacterium glutamicum
ATCC 13032, comprising argJ, argB and argD as well as part of argC an
d argF, has been cloned by heterologous complementation of an Escheric
hia 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 promot
er located in the coding part of the preceding argJ gene, whereas tran
scription 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 corr
esponding N-acetylglutamate kinase activity was observed both in cell
extracts of C. glutamicum and in recombinant E. coil argB auxotrophic
strains. Extracts of E. coli cells carrying cloned corynebacterial DNA
display an ornithine acetyltransferase activity (encoded by argJ) whi
ch alleviates the acetylornithinase (encoded by argE) deficiency of th
e enterobacterial host. In contrast to Bacillus stearothermophilus orn
ithine acetyltransferase which also exhibits acetylglutamate synthase
activity, C. glutamicum ornithine acetyltransferase appears monofuncti
onal. ArgA and ArgB proteins from different sources share highly signi
ficant similarities. The evolutionary implications of these data are d
iscussed.