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ID 48608
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creator
Hasegawa, Jun
Uchiyama, Susumu
Tanimoto, Yuko
Mizutani, Masayuki
Kobayashi, Yuji
Igarashi, Yasuo
abstract
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.
description
This work was supported by a grant from the Japanese Ministry of Education, Science and Culture.
journal title
Journal of Biological Chemistry
volume
Volume 275
issue
Issue 48
start page
37824
end page
37828
date of issued
2000-12-01
publisher
The American Society for Biochemistry and Molecular Biology, Inc.
issn
0021-9258
1083-351X
publisher doi
language
eng
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
publisher
rights
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.
relation url
department
Graduate School of Integrated Sciences for Life