Cooperation of Sly1/SM-Family Protein and Sec18/NSF of Saccharomyces cerevisiae in Disassembly of cis-SNARE Membrane-Protein Complexes(Biochemistry & Molecular Biology)
スポンサーリンク
概要
- 論文の詳細を見る
Assembly and disassembly of the SNARE membraneprotein complexes plays a key role in vesicular trafficking. The SM-family Sly1 protein binds to the tSNARE Sed5 protein and stimulates its assembly into a trans-SNARE complex. Disassembly of the resulting cis-SNARE complex containing Sed5 was retarded in a temperature-sensitive yeast mutant of Sly1 protein with a defect in binding to Sed5. A temperature-sensitive mutation (sec18-1) of Sec18/NSF disassembly ATPase showed synthetic lethality with the sly1^<ts> mutation. These results suggest that Sly1 and Sec18 proteins work cooperatively and that the binding of Sly1 to Sed5 stimulates the disassembly of the cis-SNARE complex by Sec18 ATPase.
- 社団法人日本農芸化学会の論文
- 2003-02-23
著者
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YODA Koji
Department of Biotechnology, University of Tokyo
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Adachi Hideya
Department Of Biofunctional Chemistry Faculty Of Agriculture Kobe University
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Yoda K
Univ. Tokyo Tokyo Jpn
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Yoda Koji
Department Of Biotechnology University Of Tokyo
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KOSODO Yoichi
Department of Biotechnology, University of Tokyo
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NODA Yoichi
Department of Biotechnology, University of Tokyo
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ADACHI Hiroyuki
Department of Biotechnology, University of Tokyo
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Yamane K
Univ. Tsukuba
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Kosodo Yoichi
Department Of Biotechnology University Of Tokyo
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Noda Y
Univ. Tokyo Tokyo Jpn
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Noda Y
Department Of Gynecology And Obstetrics Kyoto University Faculty Of Medicine
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Yoda Koji
Department Of Agricultural Chemistry The University Of Tokyo
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Adachi Hiroyuki
Department Of Biotechnology Graduate School Of Agricultural And Life Sciences University Of Tokyo
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Noda Yoichi
Department Of Biotechnology University Of Tokyo
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Yoda K
Institute Of Biological Sciences University Of Tsukuba
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