Difference between revisions of "Part:BBa K902030"
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| − | <html> The mntR metalloregulatory protein is native to the Escherichia coli K-12 strain. This transcriptional regulator is found to observe the level of manganese and responds accordingly. The structure of this protein consists of a metal-binding domain that will respond in the presence of manganese and repress the small RNA gene mntS. Lack of mntS will then repress the manganese ion transporter (mntH) as 42-amino-acid protein forms. When this protein membrane is | + | <html> The mntR metalloregulatory protein is native to the Escherichia coli K-12 strain. This transcriptional regulator is found to observe the level of manganese and responds accordingly. The structure of this protein consists of a metal-binding domain that will respond in the presence of manganese and repress the small RNA gene mntS. Lack of mntS will then repress the manganese ion transporter (mntH) as 42-amino-acid protein forms. When this protein membrane is repressed the bacteria cannot gain the needed manganese. It is also found that the mntR positively regulates the mntP a putative efflux pump that regulates the intracellular level of manganese.</p></html> |
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Latest revision as of 02:01, 27 October 2012
Manganese homeostatic regulation (mntR)
The mntR metalloregulatory protein is native to the Escherichia coli K-12 strain. This transcriptional regulator is found to observe the level of manganese and responds accordingly. The structure of this protein consists of a metal-binding domain that will respond in the presence of manganese and repress the small RNA gene mntS. Lack of mntS will then repress the manganese ion transporter (mntH) as 42-amino-acid protein forms. When this protein membrane is repressed the bacteria cannot gain the needed manganese. It is also found that the mntR positively regulates the mntP a putative efflux pump that regulates the intracellular level of manganese.
Sequence and Features