dc.contributor.author |
Xiang, H |
en |
dc.contributor.author |
Ishibashi, K |
en |
dc.contributor.author |
Nishikiori, M |
en |
dc.contributor.author |
Vista, Mauren |
en |
dc.contributor.author |
Ishikawa, M |
en |
dc.contributor.author |
Katoh, E |
en |
dc.coverage.spatial |
United States |
en |
dc.date.accessioned |
2012-05-24T21:00:25Z |
en |
dc.date.issued |
2012-01 |
en |
dc.identifier.citation |
Protein Expression and Purification 81(1):89-95 Jan 2012 |
en |
dc.identifier.issn |
1046-5928 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/18379 |
en |
dc.description.abstract |
Tomato mosaic virus (genus, Tobamovirus) is a member of the alphavirus-like superfamily of positive-strand RNA viruses, which include many plant and animal viruses of agronomical and clinical importance. The RNA of alphavirus-like superfamily members encodes replication-associated proteins that contain a putative superfamily 1 helicase domain. To date, a viral three-dimensional superfamily 1 helicase structure has not been solved. For the study reported herein, we expressed tomato mosaic virus replication proteins that contain the putative helicase domain and additional upstream N-terminal residues in Escherichia coli. We found that an additional 155 residues upstream of the N-terminus of the helicase domain were necessary for stability. We developed an efficient procedure for the expression and purification of this fragment and have examined factors that affect its stability. Finally, we also showed that the stable fragment has nucleoside 5'-triphosphatase activity. |
en |
dc.language |
eng |
en |
dc.publisher |
Elsevier; Academic Press |
en |
dc.relation.ispartofseries |
Protein Expression and Purification |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/1046-5928/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
Adenosine Triphosphate |
en |
dc.subject |
Amino Acid Sequence |
en |
dc.subject |
Electrophoresis, Polyacrylamide Gel |
en |
dc.subject |
Escherichia coli |
en |
dc.subject |
Molecular Sequence Data |
en |
dc.subject |
Protein Stability |
en |
dc.subject |
Protein Structure, Tertiary |
en |
dc.subject |
RNA Helicases |
en |
dc.subject |
Recombinant Proteins |
en |
dc.subject |
Tobamovirus |
en |
dc.subject |
Viral Proteins |
en |
dc.title |
Expression, purification, and functional characterization of a stable helicase domain from a tomato mosaic virus replication protein. |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1016/j.pep.2011.09.002 |
en |
pubs.issue |
1 |
en |
pubs.begin-page |
89 |
en |
pubs.volume |
81 |
en |
dc.rights.holder |
Copyright: Elsevier; Academic Press |
en |
dc.identifier.pmid |
21964444 |
en |
pubs.end-page |
95 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
234341 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
dc.identifier.eissn |
1096-0279 |
en |
dc.identifier.pii |
S1046-5928(11)00249-X |
en |
pubs.record-created-at-source-date |
2012-05-25 |
en |
pubs.dimensions-id |
21964444 |
en |