Functional Expression and Site-Directed Mutagenesis of Photoactive Yellow Protein.
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概要
- 論文の詳細を見る
The gene encoding photoactive yellow protein (PYP) was isolated from Ectothiorhodospira halophila, and a high-level expression system for PYP was constructed in Escherichia coli. The molecular weight and the absorption spectrum of PYP expressed in E. coli were identical with those of the native PYP isolated from E. halophila. The amino acid residues which might interact with the chromophore (Tyr42, Glu46, Thr50, Arg52, and Cys69) were mutated by site-directed mutagenesis and the absorption spectra of these mutants were exmained to study the chromophore/protein interaction in PYP. The former three substitutions (Y42F, E46Q, and T50V) Brought about no change and that of Cys69 (C69S) led to no formation of pigments. These results suggest that Tyr42, Glu46, and Thr50 strongly interact with the chromophore, while Arg52 does not contribute the color tuning of PYP.
- 社団法人 日本生化学会の論文
著者
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Imamoto Yasushi
Department Of Biophysics Graduate School Of Science Kyoto University
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Tokunaga Fumio
Department Of Biology Graduate School Of Science Osaka Univercity:japan Science And Technology Agenc
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Kataoka Mikio
Department Of Cancer Immunotherapy Osaka University Graduate School Of Medicine
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Imamoto Yasushi
Department of Earth and Space Science, Graduate School of Science, Osaka University
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Hisatiomi Osamu
Department of Earth and Space Science, Graduate School of Science, Osaka University
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