Comparative Complete Genome Sequence Analysis of the Amino Acid Replacements Responsible for the Thermostability ofCorynebacterium efficiens | Zendy

Yousuke Nishio | Zendy; Yoji Nakamura | Zendy; Yutaka Kawarabayasi | Zendy; Yoshihiro Usuda | Zendy; Eiichiro Kimura | Zendy; Shinichi Sugimoto | Zendy; Kazuhiko Matsui | Zendy; Akihiko Yamagishi | Zendy; Hisashi Kikuchi | Zendy; Kazuho Ikeo | Zendy; Takashi Gojobori | Zendy

Open Access

Comparative Complete Genome Sequence Analysis of the Amino Acid Replacements Responsible for the Thermostability ofCorynebacterium efficiens

Author(s) -

Yousuke Nishio,

Yoji Nakamura,

Yutaka Kawarabayasi,

Yoshihiro Usuda,

Eiichiro Kimura,

Shinichi Sugimoto,

Kazuhiko Matsui,

Akihiko Yamagishi,

Hisashi Kikuchi,

Kazuho Ikeo,

Takashi Gojobori

Publication year - 2003

Publication title -

genome research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.556

H-Index - 297

eISSN - 1549-5469

pISSN - 1088-9051

DOI - 10.1101/gr.1285603

Subject(s) - corynebacterium glutamicum , thermostability , biology , amino acid , gc content , threonine , serine , genetics , genome , alanine , orfs , biochemistry , corynebacterium , peptide sequence , gene , open reading frame , bacteria , enzyme , phosphorylation

Corynebacterium efficiens is the closest relative of Corynebacterium glutamicum, a species widely used for the industrial production of amino acids. C. efficiens but not C. glutamicum can grow above 40 degrees C. We sequenced the complete C. efficiens genome to investigate the basis of its thermostability by comparing its genome with that of C. glutamicum. The difference in GC content between the species was reflected in codon usage and nucleotide substitutions. Our comparative genomic study clearly showed that there was tremendous bias in amino acid substitutions in all orthologous ORFs. Analysis of the direction of the amino acid substitutions suggested that three substitutions are important for the stability of the C. efficiens proteins: from lysine to arginine, serine to alanine, and serine to threonine. Our results strongly suggest that the accumulation of these three types of amino acid substitutions correlates with the acquisition of thermostability and is responsible for the greater GC content of C. efficiens.

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