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Adaptations of protein structure and function to temperature: there is more than one way to 'skin a cat'

文献类型： 外文期刊

作者： Fields, Peter A. 1 ; Dong, Yunwei 2 ; Meng, Xianliang 3 ; Somero, George N. 4 ;

作者机构： 1.Franklin & Marshall Coll, Dept Biol, Lancaster, PA 17603 USA

2.Xiamen Univ, State Key Lab Marine Environm Sci, Xiamen 361005, Peoples R China

3.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao 266071, Peoples R China

4.Stanford Univ, Dept Biol, Hopkins Marine Stn, Pacific Grove, CA 93940 USA

关键词： A(4)-lactate dehydrogenase;Cytosolic malate dehydrogenase;Protein stability;Temperature adaptation

期刊名称：JOURNAL OF EXPERIMENTAL BIOLOGY （ 影响因子：3.312； 五年影响因子：3.828 ）

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收录情况： SCI

摘要： Sensitivity to temperature helps determine the success of organisms in all habitats, and is caused by the susceptibility of biochemical processes, including enzyme function, to temperature change. A series of studies using two structurally and catalytically related enzymes, A(4)-lactate dehydrogenase (A(4)-LDH) and cytosolic malate dehydrogenase (cMDH) have been especially valuable in determining the functional attributes of enzymes most sensitive to temperature, and identifying amino acid substitutions that lead to changes in those attributes. The results of these efforts indicate that ligand binding affinity and catalytic rate are key targets during temperature adaptation: ligand affinity decreases during cold adaptation to allow more rapid catalysis. Structural changes causing these functional shifts often comprise only a single amino acid substitution in an enzyme subunit containing approximately 330 residues; they occur on the surface of the protein in or near regions of the enzyme that move during catalysis, but not in the active site; and they decrease stability in cold-adapted orthologs by altering intra-molecular hydrogen bonding patterns or interactions with the solvent. Despite these structure-function insights, we currently are unable to predict a priori how a particular substitution alters enzyme function in relation to temperature. A predictive ability of this nature might allow a proteome-wide survey of adaptation to temperature and reveal what fraction of the proteome may need to adapt to temperature changes of the order predicted by global warming models. Approaches employing algorithms that calculate changes in protein stability in response to a mutation have the potential to help predict temperature adaptation in enzymes; however, using examples of temperature adaptive mutations in A(4)-LDH and cMDH, we find that the algorithms we tested currently lack the sensitivity to detect the small changes in flexibility that are central to enzyme adaptation to temperature.

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