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 journalArticle

143 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)2662-2666
Number of pages5
JournalJournal of Biological Chemistry
Volume268
Issue number4
StatePublished - Feb 5 1993
Externally publishedYes

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N-Ethylmaleimide-Sensitive Proteins
Adenosine Triphosphatases
Dissection
Ethylmaleimide
Consensus Sequence
Protein Transport
Cricetulus
Escherichia coli
Sequence Analysis
Ovary
Nucleotides
Adenosine Triphosphate
Monoclonal Antibodies
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. / Tagaya, Mitsuo; Wilson, Duncan W.; Brunner, Michael; Arango, Nancy; Rothman, James E.

In: Journal of Biological Chemistry, Vol. 268, No. 4, 05.02.1993, p. 2662-2666.

Research output: Contribution to journalArticle

Tagaya, Mitsuo ; Wilson, Duncan W. ; Brunner, Michael ; Arango, Nancy ; Rothman, James E. / Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. In: Journal of Biological Chemistry. 1993 ; Vol. 268, No. 4. pp. 2662-2666.
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