Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability.

Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability. Research Abstract Details 

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Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability. Abstract Text:

Yoshihiro Sambongi,Susumu Uchiyama,Yuji Kobayashi,Yasuo Igarashi,Jun Hasegawa,

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. Mutagenesis and structure analyses based on comparative studies using a thermophile Hydrogenobacter thermophilus cytochrome c-552 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.

Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability. Publishing Authors By Initials

Y Sambongi,S Uchiyama,Y Kobayashi,Y Igarashi,J Hasegawa,

For similar biological phenomena, cell phenomena, and immunity: immunity: antibody specificity: species specificity research abstracts see: biological phenomena, cell phenomena, and immunity: immunity: antibody specificity: species specificity research

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Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability. Journal Published:

PUBLICATION TYPE: Review

Journal: European journal of biochemistry / FEBS

VOLUME: 269

Page Numbers: 3355-61

Journal Abbreviation: Eur. J. Biochem.

ISSN: 0014-2956

DAY: 21

MONTH: Jul

YEAR: 2002

Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability. Information

Number of References: 42

LANGUAGE: eng

NlmUniqueID: 107600

Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability. Keywords Mesh Terms:

KEYWORDS: Species Specificity

MESH TERMS: biosynthesis

Chemical & Substance for Abstract: Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability. Information

Substance Name: Protein Disulfide-Isomerase

Registry Number: EC 5.3.4.1

Grant and Affiliation Information for Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability.

AFFILIATION: Graduate School of Biosphere Sciences, Hiroshima University, Higashi-Hiroshima, Japan. sambongi@hiroshima-u.ac.jp

Country: Germany

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MEDLINETA: Eur J Biochem

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