Authors: Seulgi Yun EunGyeong Lee SangYoon Kim Jong Moon Shin Won Seok Jung DooByoung Oh Sang Yup Lee Ohsuk Kwon
Publish Date: 2014/09/18
Volume: 70, Issue: 1, Pages: 103-109
Abstract
In this study we characterized the CpxRA twocomponent signal transduction system of the rumen bacterium Mannheimia succiniciproducens The truncated form of the CpxA sensor kinase protein without its transmembrane domain was able to autophosphorylate and transphosphorylate the CpxR response regulator protein in vitro We identified 152 putative target genes for the Cpx system in M succiniciproducens which were differentially expressed by more than twofold upon overexpression of the CpxR protein Genes of a putative 16gene operon related to the cell wall and lipopolysaccharide biosynthesis were induced strongly upon CpxR overexpression The promoter region of the first gene of this operon wecC encoding UDPNacetylDmannosaminuronate dehydrogenase was analyzed and found to contain a sequence homologous to the CpxR box of Escherichia coli An electrophoretic mobility shift assay showed that the phosphorylated CpxR proteins were able to bind specifically to PCRamplified DNA fragments containing the promoter sequence of wecC Furthermore a cpxRdisrupted mutant strain exhibited increased envelope permeability compared with a wildtype strain These results suggest that the Cpx system of M succiniciproducens is involved in the maintenance of the integrity of the cell envelopeThis work was supported by Grants 20110031947 and 20110031963 from the Intelligent Synthetic Biology Global Frontier Program of the National Research Foundation and by a Grant from the NextGeneration BioGreen 21 Program PJ00952402 of the Rural Development Administration Republic of Korea
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