the genomics of disulfide bonding and protein stabilization in thermophiles二硫键的基因组学和蛋白质在嗜热菌稳定.pdfVIP

Open access, freely available online PLoS BIOLOGY The Genomics of Disulfide Bonding and Protein Stabilization in Thermophiles 1,2[ 3[ 1 3 1 1,2,3* Morgan Beeby , Brian D. O’Connor , Carsten Ryttersgaard , Daniel R. Boutz , L. Jeanne Perry , Todd O. Yeates 1 UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California, United States of America, 2 Department of Chemistry and Biochemistry, University of California, Los Angeles, California, United States of America, 3 Molecular Biology Institute, University of California, Los Angeles, California, United States of America 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 proteins matching this target phylogenetic profile singles out a specific protein, known as protein disulfide oxidoreductase, as a potential key player in thermophilic intracel