文摘
To further our understanding of the biology of the thermophilic bacterium Geobacillus thermoleovoransT80, we now report the first proteomic analysis of the insoluble subproteome of this isolate. Acombination of both shotgun and multidimensional methodologies were utilized, and a total of 8628peptides was initially identified by automated MS/MS identification software. Curation of these peptidesled to a final list of 184 positive protein identifications. The proteins from this insoluble subproteomewere functionally classified, and physiochemical characterization was carried out. Of 15 hypotheticalconserved proteins identified, we have assigned function to all but four. A total of 31 proteins werepredicted to possess signal peptides. In silico investigation of these proteins allowed us to identifyfour of the five bacterial classes of signal peptide, namely, (i) twin-arginine translocation; (ii) Sec-type;(iii) lipoprotein, and (iv) ABC transport. In addition, a number of proteins were identified that are knownto be involved in the transport of compatible solutes, known to be important in microbial stressresponses.