Mimicking the evolution of a thermally stable monomeric four-helix bundle by fusion of four identical single-helix peptides

Satoshi Akanuma, Taku Matsuba, Emi Ueno, Naoki Umeda, Akihiko Yamagishi

研究成果: Article査読

17 被引用数 (Scopus)

抄録

Internal symmetry is a common feature of the tertiary structures of proteins and protein domains. Probably, because the genes of homo-oligomeric proteins duplicated and fused, their evolutionary descendants are proteins with internal symmetry. To identify any advantages that cause monomeric proteins with internal symmetry to be selected evolutionarily, we characterized some of the physical properties of a recombinant protein with a sequence consisting of two tandemly fused copies of the Escherichia coli Lac repressor C-terminal α-helix. This polypeptide exists in solution mainly as dimer that likely maintains a four-helix bundle motif. Thermal unfolding experiments demonstrate that the protein is considerably more stable at elevated temperatures than is a homotetramer consisting of four non-covalently associated copies of a 21-residue polypeptide similar in sequence to that of the Lac repressor C-terminal α-helix. A tandem duplication of our helix-loop-helix polypeptide yields an even more thermally stable protein. Our results exemplify the concept that fusion of non-covalently assembled polypeptide chains leads to enhanced protein stability. Herein, we discuss how our work relates to the evolutionary selective-advantages realized when symmetrical homo-oligomers evolve into monomers. Moreover, our thermally stable single-chain four-helix bundle protein may provide a robust scaffold for development of new biomaterials.

本文言語English
ページ(範囲)371-379
ページ数9
ジャーナルJournal of biochemistry
147
3
DOI
出版ステータスPublished - 2010 3
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学

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