Abstract
ImmersedImmersed in waters saltier than chicken soup, salt-tolerant “halophilic” microorganisms are able to thrive in conditions that would reduce a less-adapted organism to a shriveled remnant. One way halophilic archaea avoid this fate is by bathing their molecular machinery in a similarly salty intracellular environment that would cause ordinary proteins to lose their shape. How do the proteins inside these cells survive?
Highlights
Immersed in waters saltier than chicken soup, salt-tolerant ‘‘halophilic’’ microorganisms are able to thrive in conditions that would reduce a less-adapted organism to a shriveled remnant
At least part of the answer seems to relate to an abundance of certain amino acid residues on the protein surface
Salttolerant proteins tend to have lots of aspartic acid, glutamic acid, and other non-hydrophobic residues on their surfaces. They tend to have fewer lysines than similar proteins from non-halophilic counterparts, their places often being taken by bulkier arginine instead
Summary
Immersed in waters saltier than chicken soup, salt-tolerant ‘‘halophilic’’ microorganisms are able to thrive in conditions that would reduce a less-adapted organism to a shriveled remnant. At least part of the answer seems to relate to an abundance of certain amino acid residues on the protein surface. Another suggests it’s not so much charge as the size of the side chain that gives these residues their evolutionary edge in a saline setting.
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