Glycine-15 in the bend between two alpha-helices can explain the thermostability of DNA binding protein HU from Bacillus stearothermophilus

Authors :: Kawamura, Shunsuke
Kakuta, Yoshimitsu
Tanaka, Isao
Hikichi, Kunio
Kuhara, Satoru
Yamasaki, Nobuyuki
Kimura, Makoto
Source :: Biochemistry. Jan 30, 1996, Vol. 35 Issue 4, p1195, 6 p.
Publication Year :: 1996
Abstract: Three mutants of Bacillus stearothermophilus DNA binding protein HU (BstHU) were developed and studied to determine how the change in amino acid residues affect its thermostability. The mutants were generated by substituting the two threonine residues and glycine-15 in BstHU by their counterparts in Bacillus subtilis DNA binding protein HU. Glycine-15 was found to contribute to the thermostability of BstHU.

Subjects :: Bacterial genetics -- Research
DNA binding proteins -- Research
Biological sciences
Chemistry

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