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ID 48608
本文ファイル
著者
Hasegawa, Jun
Uchiyama, Susumu
Tanimoto, Yuko
Mizutani, Masayuki
Kobayashi, Yuji
Igarashi, Yasuo
抄録(英)
Mesophilic cytochrome c551 of Pseudomonas aeruginosa (PA c551) became as stable as its thermophilic counterpart, Hydrogenobacter thermophilus cytochrome c552 (HT c552), through only five amino acid substitutions. The five residues, distributed in three spatially separated regions, were selected and mutated with reference to the corresponding residues in HT c552 through careful structure comparison. Thermodynamic analysis indicated that the stability of the quintuple mutant of PA c551 could be partly attained through an enthalpic factor. The solution structure of the mutant showed that, as in HT c552, there were tighter side chain packings in the mutated regions. Furthermore, the mutant had an increased total accessible surface area, resulting in great negative hydration free energy. Our results provide a novel example of protein stabilization in that limited amino acid substitutions can confer the overall stability of a natural highly thermophilic protein upon a mesophilic molecule.
内容記述
This work was supported by a grant from the Japanese Ministry of Education, Science and Culture.
掲載誌名
Journal of Biological Chemistry
275巻
48号
開始ページ
37824
終了ページ
37828
出版年月日
2000-12-01
出版者
The American Society for Biochemistry and Molecular Biology, Inc.
ISSN
0021-9258
1083-351X
出版者DOI
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
publisher
権利情報
This research was originally published in the Journal of Biological Chemistry. Jun Hasegawa, Susumu Uchiyama, Yuko Tanimoto, Masayuki Mizutani, Yuji Kobayashi, Yoshihiro Sambongi and Yasuo Igarashi. Selected Mutations in a Mesophilic Cytochrome c Confer the Stability of a Thermophilic Counterpart. J. Biol. Chem. 2000; 275(48):37824-37828. © the American Society for Biochemistry and Molecular Biology.
関連情報URL
部局名
統合生命科学研究科