The role of EIIMan and CcpA in the regulation of urease expression in Streptococcus salivarius 57.I

碩士 === 長庚大學 === 生物醫學研究所 === 105 === Streptococcus salivarius is the major ureolytic microbe in the human mouth, and the expression of urease in strain 57.I is upregulated at acidic growth pH and under glucose excess. Earlier studies indicate that the enzyme II (EIIMan) of the phosphoenolpyruvate: ma...

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Bibliographic Details
Main Authors: Yu Hsiang Shen, 沈育湘
Other Authors: Y. Y. M. Chen
Format: Others
Language:en_US
Published: 2017
Online Access:http://ndltd.ncl.edu.tw/handle/vc6s25
Description
Summary:碩士 === 長庚大學 === 生物醫學研究所 === 105 === Streptococcus salivarius is the major ureolytic microbe in the human mouth, and the expression of urease in strain 57.I is upregulated at acidic growth pH and under glucose excess. Earlier studies indicate that the enzyme II (EIIMan) of the phosphoenolpyruvate: mannose phosphotransferase system (Man-PTS), the enzyme I of PTS and CcpA all participate in urease regulation. This study revealed that CcpA repressed manL expression, gene encoding the light form of EIIMan in cells grown in galactose, suggesting that CcpA regulates urease expression, at least in part, by controlling manL expression. By using the chemostat culture system and a manL- and a manL-manH (encoding the heavy form of EIIMan) double knockout derivatives of S. salivarius 57.I, and a manH-deficient derivative of the codY-deficient S. salivarius, it was found that, in the absence of codY, ManL and ManH repress the urease activity in cells grown at neutral pH, indicating that Man-PTS only fine tunes urease expression. As both acidic pH and excess lactose upregulated non-phosphorylated ManH production, it is suggested that when less amount of phosphorylated ManH is available for regulation, the repression by Man-PTS on urease is greatly reduced.