 |
|
Title
|
 |
Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport.
|
 |
|
Authors
|
 |
M.Tagaya,
D.W.Wilson,
M.Brunner,
N.Arango,
J.E.Rothman.
|
 |
|
Ref.
|
 |
J Biol Chem, 1993,
268,
2662-2666.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
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.
|
 |
 |
 |