Mj. Danson et Dw. Hough, THE STRUCTURAL BASIS OF PROTEIN HALOPHILICITY, Comparative biochemistry and physiology. Section A: Comparative physiology, 117(3), 1997, pp. 307-312
Citations number
31
Categorie Soggetti
Physiology,Biology
Journal title
Comparative biochemistry and physiology. Section A: Comparative physiology
The halophilic Archaea live in hypersaline environments and maintain a
n osmotic balance by accumulating intracellular concentrations of salt
(mainly KCI) that are isotonic with the exterior. Therefore, their ce
llular components are adapted to concentrations of KCl approaching 5 M
and often require these levels of salt for stability and function. He
re, we consider the effects of hypersalinity on protein structure and
then review the known structures of proteins from the halophilic Archa
ea in the context of these effects. Specific proteins considered are f
erredoxin, malate dehydrogenase, dihydrofolate reductase, dihydrolipoa
mide dehydrogenase nase and elongation factor Tu. From the available d
ata, models for the structural basis of halophilicity are discussed an
d analysed. (C) 1997 Elsevier Science Inc.