Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Notes
Cooperation of Sly1/SM-Family Protein and Sec18/NSF of Saccharomyces cerevisiae in Disassembly of cis-SNARE Membrane-Protein Complexes
Yoichi KOSODOYoichi NODAHiroyuki ADACHIKoji YODA
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2003 年 67 巻 2 号 p. 448-450

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  Assembly and disassembly of the SNARE membrane-protein 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 sly1ts 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.
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© 2003 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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