Functional analysis of L-serine O-acetyltransferase from Corynebacterium glutamicum.
We report here the function of L-serine O-acetyltransferase (SAT) from the glutamic acid-producing bacterium Corynebacterium glutamicum. Based on the genome sequence of C. glutamicum and the NH(2)-terminal amino-acid sequence, the gene encoding SAT (cysE) was cloned and expressed in C. glutamicum. Deletion analysis of the 5'-noncoding region showed a putative -10 region ((-27)TTAAGT(-22) or (-26)TAAGTC(-21)) and a possible ribosome-binding site ((-12)AGA(-10)) just upstream from the start codon. We found that the SAT activity was sensitive to feedback inhibition by L-cysteine, and that SAT synthesis was repressed by L-methionine. Further, cysE-disrupted cells showed L-cysteine auxotrophy, indicating that C. glutamicum synthesizes L-cysteine from L-serine via O-acetyl-L-serine through the pathway involving SAT and O-acetyl-L-serine sulfhydrylase in the same manner as Escherichia coli.
Haitani
Yutaka
Y
Department of Bioscience, Fukui Prefectural University, Fukui, Japan.
Awano
Naoki
N
Yamazaki
Mizue
M
Wada
Masaru
M
Nakamori
Shigeru
S
Takagi
Hiroshi
H
D003001:Cloning, Molecular; D048230:Corynebacterium glutamicum / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D008969:Molecular Sequence Data; D051050:Serine O-Acetyltransferase / Q000737:chemistry / Q000378:metabolism*
D051050:Serine O-Acetyltransferase