The DNA Binding Domains of Transcription Factors, PhoB and OmpR, Adopt the Same Folding as that of Histone H5 and Bind to RNA Polymerase Using the Ends of Two .ALPHA.-Helices.
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概要
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A possible structure and possible DNA-binding mode of transcription factors in the PhoB/OmpR family are discussed in comparison with those of another DNA-binding protein, histone H5. The amino acid sequences of the DNA-binding domains of factors in this family strongly resemble that of H5 and thus the former are predicted to adopt the same globular fold as the latter, i.e. a domain which is composed of three α-helices, a β-strand (placed between the first two helices) and a β-hairpin at the C-terminus (the β-strand and the β-hairpin fold into a single β-sheet). The third helix is predicted to contact the DNA bases. The residues which have been identified as contacting RNA polymerase are located at the C-terminus of the second helix and the N-terminus of the third helix.
- 日本学士院の論文
著者
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SUZUKI Masashi
MRC Lab. of Mol. Biol.
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MAKINO Kozo
The Research Institute for Microbial Diseases, Osaka University
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