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Hyper‐thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C
Author(s) -
Tanaka Tomoyuki,
Sawano Masahide,
Ogasahara Kyoko,
Sakaguchi Yasushi,
Bagautdinov Bagautdin,
Katoh Etsuko,
Kuroishi Chizu,
Shinkai Akeo,
Yokoyama Shigeyuki,
Yutani Katsuhide
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.06.084
Subject(s) - pyrococcus horikoshii , thermus thermophilus , thermostability , crystallography , chemistry , denaturation (fissile materials) , crystal structure , escherichia coli , biochemistry , nuclear chemistry , enzyme , gene
We found that the CutA1 protein, from Pyrococcus horikoshii ( Ph CutA1), has an extremely high denaturation temperature ( T d ) of nearly 150 °C, which exceeds the highest record determined by DSC by about 30 °C. To elucidate the mechanism of the ultra‐high stability of Ph CutA1, we analyzed the crystal structures of CutA1 proteins from three different sources, P. horikoshii , Thermus thermophilus , and Escherichia coli , with different growth temperatures (98, 75, and 37 °C). This analysis revealed that the remarkably increased number of ion pairs in the monomeric structure contributes to the stabilization of the trimeric structure and plays an important role in enhancing the T d , up to 150 °C, for Ph CutA1.