TAILIEUCHUNG - Báo cáo Y học: Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability

Cytochrome c is widely distributed in bacterial species, from mesophiles to thermophiles, and is one of the best-characterized redox proteins in terms of biogenesis, folding, structure, function, and evolution. Experimental molecular biology techniques (gene cloning and expression) have become applicable to cytochrome c, enabling its engineering and manipulation. Heterologous expression systems for cytochromes c in bacteria, for use in mutagenesis studies, have been established by extensive investigation of the biological process by which the functional structure is formed. . | Eur. J. Biochem. 269 _V5_ - _W1 2002 FEBS 2002 doi REVIEW ARTICLE Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation folding and stability Yoshihiro Sambonai1. Susumu Uchivama2 Yuji Kobavashi2. Yasuo Iaarashi3 and Jun Haseaawa4 Graduate School of Biosphere Sciences Hiroshima University Japan 2Faculty of Pharmaceutical Science Osaka University Japan 3Department of Biotechnology University of Tokyo Japan 4Daiichi Pharmaceutical Co. Ltd Tokyo Japan Cytochrome c is widely distributed in bacterial species from mesophiles to thermophiles and is one of the hetOcharac-terized redox proteins in terms of biogenesis foldings structure. function and 6 111 1011. molecular biology techniques gene cloning and expression have become applicable to cytochrome c enabling its engineering and manipulation. Heterologous expression systems for cytochromes c in bacteria oor use in mutagenesis studies have been established by extensive investigation of the biological process by which the functional structure is formed. Mutagenesis and structure analyses based on comparative studies using a thermophile Hydrogenobacter thermophilus cytochrome c-kk2 and its mesophilic counterpart have provided substantial clues to the mechanism underlying protein stability at the amino-acid level. The molecular mechanisms underlying protein maturation folding and stability in bacterial cytochromes c are beginning to be understood. Keywords bacteria biogenesis cytochrome c Hydrogeno-bacter thermophilus mutations protein stability. In mitochondria electoons shuttìe between the 11 111 111 -bound cytochrome bc1 complex and cytochrome oxidase via a water-soluble protein cytochrome c. This process is required for generation of an electrochemical proton gradient across the membrane proton-motive force which drives the synthesis of ATP a 0 1 nnrrgy currency. Bacteria also have soluble monoheme Class I cytochromes c

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