The genomics of disulfide bonding and protein stabilization in thermophiles.

ABSTRACT: Thermophilic organisms flourish in varied high-temperature environmental niches that are deadly to other organisms. Recently, genomic evidence has implicated a critical role for disulfide bonds in the structural stabilization of intracellular proteins from certain of these organisms, contrary to the conventional view that structural disulfide bonds are exclusively extracellular. Here both computational and structural data are presented to explore the occurrence of disulfide bonds as a protein-stabilization method across many thermophilic prokaryotes. Based on computational studies, disulfide-bond richness is found to be widespread, with thermophiles containing the highest levels. Interestingly, only a distinct subset of thermophiles exhibit this property. A computational search for protein

SUBMITTER: Beeby M 

PROVIDER: S-EPMC1188242 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature