Proline reduces the binding of transcriptional regulator ArgR to upstream of argB in Corynebacterium glutamicum

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 cont...

Full description

Saved in:
Bibliographic Details
Published in:Applied microbiology and biotechnology 2010-03, Vol.86 (1), p.235-242
Main Authors: Lee, Soo Youn, Shin, Hwa Sung, Park, Jin-Soo, Kim, Yang-Hoon, Min, Jiho
Format: Article
Language:English
Subjects:
Applied Genetics and Molecular Biotechnology
Arginine - metabolism
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding Sites
Biological and medical sciences
Biomedical and Life Sciences
Biosynthesis
Biotechnology
Chromatin Immunoprecipitation
Chromosomes
Corynebacterium glutamicum - genetics
Corynebacterium glutamicum - metabolism
E coli
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation, Bacterial
Genetic engineering
Glutamic Acid - metabolism
Kinases
Life Sciences
Microbial Genetics and Genomics
Microbiology
Operon
Ornithine - metabolism
Plasmids
Proline - metabolism
Protein Binding - drug effects
Proteins
Repressor Proteins - genetics
Repressor Proteins - metabolism
Studies
Upstream
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-009-2264-5