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Delving into the molecular mechanism behind deep-sea bacteria's pressure tolerance
Date:7/26/2012

the active site of IPMDH is unique.

"At the site of the penetration, there is a difference of amino acid between IPMDHs from bacteria that thrive in high-pressure environments and those that are sensitive to it. Based on this data, we substituted one amino acid at the site of the IPMDH from pressure-sensitive bacteria and checked its activity under pressure," says Watanabe. "And as we expected, only this one residue-substituted IPMDH, which has 364 amino acids in total, achieved pressure resistance comparable to the bacteria that thrive in high-pressure environments."

This means that it may soon be possible to synthesize designer pressure-resistant proteins. The team plans to continue their high-pressure studies of several other proteins to try to discover the physical principles behind pressure resistance mechanisms that enable bacteria to thrive in high-pressure conditions.


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Contact: Catherine Meyers
cmeyers@aip.org
301-209-3088
American Institute of Physics
Source:Eurekalert

Page: 1 2

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