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

M. Tagaya; D. W. Wilson; M. Brunner; N. Arango; J. E. Rothman

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

M. Tagaya, D. W. Wilson, M. Brunner, N. Arango, J. 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 - 1993
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Cite this

@article{c162321ae72845f3a7ff90970994c133,

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 = "M. Tagaya and Wilson, {D. W.} and M. Brunner and N. Arango and Rothman, {J. E.}",

year = "1993",

language = "English (US)",

volume = "268",

pages = "2662--2666",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "4",

}

TY - JOUR

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

AU - Tagaya, M.

AU - Wilson, D. W.

AU - Brunner, M.

AU - Arango, N.

AU - Rothman, J. E.

PY - 1993

Y1 - 1993

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.

UR - http://www.scopus.com/inward/record.url?scp=0027474007&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027474007&partnerID=8YFLogxK

M3 - Article

C2 - 8428942

AN - SCOPUS:0027474007

SN - 0021-9258

VL - 268

SP - 2662

EP - 2666

JO - Journal of Biological Chemistry

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

Other files and links

Fingerprint

Cite this