Functional analysis of l-serineO-acetyltransferase fromCorynebacterium glutamicum
| Autor: | Masaru Wada, Naoki Awano, Mizue Yamazaki, Hiroshi Takagi, Shigeru Nakamori, Yutaka Haitani |
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| Rok vydání: | 2006 |
| Předmět: |
biology
Auxotrophy Molecular Sequence Data Corynebacterium Gene Expression Regulation Bacterial biology.organism_classification medicine.disease_cause Microbiology Molecular biology Corynebacterium glutamicum Biochemistry Start codon Acetyltransferase Genetics medicine bacteria Serine O-acetyltransferase Cloning Molecular Serine O-Acetyltransferase Molecular Biology Escherichia coli Gene |
| Zdroj: | FEMS Microbiology Letters. 255:156-163 |
| ISSN: | 1574-6968 0378-1097 |
| DOI: | 10.1111/j.1574-6968.2005.00068.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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