Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport Journal Article
| Authors: | Tagaya, M.; Wilson, D. W.; Brunner, M.; Arango, N.; Rothman, J. E. |
| Article 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. |
| Keywords: | controlled study; nonhuman; protein domain; proteins; animal cell; animal; protein degradation; protein binding; enzyme activity; monoclonal antibody; antibodies, monoclonal; amino acid sequence; molecular sequence data; hybrid protein; escherichia coli; carrier proteins; peptide fragments; recombinant protein; protein transport; binding sites; adenosine triphosphate; protein structure; adenosine triphosphatase; biological transport; golgi complex; cho cell; cho cells; cricetinae; cricetulus griseus; membrane vesicle; golgi apparatus; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; n ethylmaleimide; macromolecular systems; adenosinetriphosphatase; hamsters; ethylmaleimide |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 268 |
| Issue: | 4 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1993-02-05 |
| Start Page: | 2662 |
| End Page: | 2666 |
| Language: | English |
| PUBMED: | 8428942 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 1 March 2019 -- Source: Scopus |
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