Identification of the substrate binding site in the N-terminal TBP-like domain of RNase H3 |
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Authors: | Miyashita Seiko Tadokoro Takashi Angkawidjaja Clement You Dong-Ju Koga Yuichi Takano Kazufumi Kanaya Shigenori |
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Institution: | Department of Material and Life Science, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan. |
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Abstract: | Ribonuclease H3 from Bacillus stearothermophilus (Bst-RNase H3) has the N-terminal TBP-like substrate-binding domain. To identify the substrate binding site in this domain, the mutant proteins of the intact protein and isolated N-domain, in which six of the seventeen residues corresponding to those involved in DNA binding of TBP are individually mutated to Ala, were constructed. All of them exhibited decreased enzymatic activities and/or substrate-binding affinities when compared to those of the parent proteins, suggesting that the N-terminal domain of RNase H3 uses the flat surface of the β-sheet for substrate binding as TBP to bind DNA. This domain may greatly change conformation upon substrate binding. |
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