期刊
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
卷 86, 期 1, 页码 235-242出版社
SPRINGER
DOI: 10.1007/s00253-009-2264-5
关键词
Proline; Upstream of argB; Corynebacterium glutamicum; ChIP assay; Ornithine
资金
- Ministry of Education, Science & Technology, Republic of Korea [11-2008-10-002-00]
- National Research Foundation of Korea [11-2008-10-002-00] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
In this study, the ArgR-binding sites on the arg operon Corynbebacterium glutamicum were characterized by in vivo chromatin immunoprecipitation (ChIP). In addition, the ArgR-binding affinity in the presence of glutamate, proline, or arginine was examined to get further information on expression control. The ChIP assay showed that the ArgR protein binds specifically to the upstream regions of argC, argB, argF, and argG. Upon proline supplementation, ArgR-binding affinity was significantly reduced upstream of argB, resulting in increased ornithine production. In contrast, there was no change in the binding affinity of ArgR to the upstream regions of argC, argF, argG, or argB following the addition of glutamate and arginine. These results suggest that the upstream region of argB on the arg operon plays an important role in interacting with ArgR under proline-supplemented conditions and that proline causes an increase in the endogenous level of ornithine by reducing the binding affinity of ArgR to the upstream region of argB.
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