Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport

Mitsuo Tagaya; Duncan W. Wilson; Michael Brunner; Nancy Arango; James E. Rothman

Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport

Mitsuo Tagaya, Duncan W. Wilson, Michael Brunner, Nancy Arango, James E. Rothman

Research output: Contribution to journal › Article › peer-review

Abstract

N-Ethylmaleimide-sensitive fusion protein (NSF) is an essential component for protein transport between Golgi cisternae. Sequence analysis and proteolytic dissection reveal that NSF contains two tandem "ATP domains," each containing the consensus sequence for the binding of nucleotide. When Escherichia coli-produced Chinese hamster ovary NSF is purified, it exhibits a low, but significant, ATPase activity. The ATPase activity of NSF is sensitive to N-ethylmaleimide and influenced by monoclonal antibodies against recombinant NSF.

Original language	English (US)
Pages (from-to)	2662-2666
Number of pages	5
Journal	Journal of Biological Chemistry
Volume	268
Issue number	4
State	Published - Feb 5 1993
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Cite this

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title = "Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport",

abstract = "N-Ethylmaleimide-sensitive fusion protein (NSF) is an essential component for protein transport between Golgi cisternae. Sequence analysis and proteolytic dissection reveal that NSF contains two tandem {"}ATP domains,{"} each containing the consensus sequence for the binding of nucleotide. When Escherichia coli-produced Chinese hamster ovary NSF is purified, it exhibits a low, but significant, ATPase activity. The ATPase activity of NSF is sensitive to N-ethylmaleimide and influenced by monoclonal antibodies against recombinant NSF.",

author = "Mitsuo Tagaya and Wilson, {Duncan W.} and Michael Brunner and Nancy Arango and Rothman, {James E.}",

year = "1993",

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language = "English (US)",

volume = "268",

pages = "2662--2666",

journal = "Journal of Biological Chemistry",

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T1 - Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport

AU - Tagaya, Mitsuo

AU - Wilson, Duncan W.

AU - Brunner, Michael

AU - Arango, Nancy

AU - Rothman, James E.

PY - 1993/2/5

Y1 - 1993/2/5

N2 - N-Ethylmaleimide-sensitive fusion protein (NSF) is an essential component for protein transport between Golgi cisternae. Sequence analysis and proteolytic dissection reveal that NSF contains two tandem "ATP domains," each containing the consensus sequence for the binding of nucleotide. When Escherichia coli-produced Chinese hamster ovary NSF is purified, it exhibits a low, but significant, ATPase activity. The ATPase activity of NSF is sensitive to N-ethylmaleimide and influenced by monoclonal antibodies against recombinant NSF.

AB - N-Ethylmaleimide-sensitive fusion protein (NSF) is an essential component for protein transport between Golgi cisternae. Sequence analysis and proteolytic dissection reveal that NSF contains two tandem "ATP domains," each containing the consensus sequence for the binding of nucleotide. When Escherichia coli-produced Chinese hamster ovary NSF is purified, it exhibits a low, but significant, ATPase activity. The ATPase activity of NSF is sensitive to N-ethylmaleimide and influenced by monoclonal antibodies against recombinant NSF.

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M3 - Article

C2 - 8428942

AN - SCOPUS:0027474007

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JF - Journal of Biological Chemistry

IS - 4

ER -

Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport

Abstract

ASJC Scopus subject areas

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