dc.contributor.author |
Gilchrist, CA |
|
dc.contributor.author |
Baker, RT |
|
dc.coverage.spatial |
Netherlands |
|
dc.date.accessioned |
2022-07-13T03:12:00Z |
|
dc.date.available |
2022-07-13T03:12:00Z |
|
dc.date.issued |
2000-09 |
|
dc.identifier.citation |
(2000). Biochimica et Biophysica Acta: international journal of biochemistry and biophysics, 1481(2), 297-309. |
|
dc.identifier.issn |
0006-3002 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/60400 |
|
dc.description.abstract |
The ubiquitin-specific proteases (Ubps) are a family of largely dissimilar enzymes with two major conserved sequence regions, containing either a conserved cysteine residue or two conserved histidine residues, respectively. The murine Unp oncoprotein and its human homologue, Unph, both contain regions similar to the conserved Cys and His boxes common to all the Ubps. In this study we show that Unp and Unph are active deubiquitinating enzymes, being able to cleave ubiquitin from both natural and engineered linear ubiquitin-protein fusions, including the polyubiquitin precursor. Mutation of the conserved Unp Cys and His residues abolishes this activity, and identifies the likely His residue in the catalytic triad. Unp is tumorigenic when overexpressed in mice, leading to the suggestion that Unp may play a role in the regulation of ubiquitin-dependent protein degradation. We have demonstrated here that the high-level expression of Unp in yeast does not disrupt the degradation of the N-end rule substrate Tyr-beta-galactosidase (betagal), the non-N-end rule substrate ubiquitin-Pro-betagal, or the degradation of abnormal, canavanine-containing proteins. These data suggest that Unp is not a general modulator of ubiquitin-dependent proteolysis. However, Unp may have a role in the regulation of the degradation of a specific, as yet undescribed, substrate(s). |
|
dc.format.medium |
Print |
|
dc.language |
eng |
|
dc.publisher |
Elsevier |
|
dc.relation.ispartofseries |
Biochimica et biophysica acta |
|
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. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
|
dc.subject |
Animals |
|
dc.subject |
Humans |
|
dc.subject |
Mice |
|
dc.subject |
Escherichia coli |
|
dc.subject |
Saccharomyces cerevisiae |
|
dc.subject |
Ubiquitin Thiolesterase |
|
dc.subject |
beta-Galactosidase |
|
dc.subject |
Endopeptidases |
|
dc.subject |
Canavanine |
|
dc.subject |
Oncogene Proteins |
|
dc.subject |
Proto-Oncogene Proteins |
|
dc.subject |
DNA, Complementary |
|
dc.subject |
Mutagenesis, Site-Directed |
|
dc.subject |
Gene Expression Regulation |
|
dc.subject |
Substrate Specificity |
|
dc.subject |
Plasmids |
|
dc.subject |
Ubiquitin-Specific Proteases |
|
dc.subject |
1 Underpinning research |
|
dc.subject |
1.1 Normal biological development and functioning |
|
dc.subject |
Generic health relevance |
|
dc.subject |
Science & Technology |
|
dc.subject |
Life Sciences & Biomedicine |
|
dc.subject |
Biochemistry & Molecular Biology |
|
dc.subject |
Biophysics |
|
dc.subject |
ubiquitin |
|
dc.subject |
ubiquitin-specific protease |
|
dc.subject |
deubiquitinating enzyme |
|
dc.subject |
proteolysis |
|
dc.subject |
Unp |
|
dc.subject |
USP4 |
|
dc.subject |
RETINOBLASTOMA GENE-PRODUCT |
|
dc.subject |
N-END RULE |
|
dc.subject |
GLUTATHIONE-S-TRANSFERASE |
|
dc.subject |
HUMAN TRE-2 ONCOGENE |
|
dc.subject |
CYCLE MUTANT TS85 |
|
dc.subject |
SACCHAROMYCES-CEREVISIAE |
|
dc.subject |
DEGRADATION SIGNAL |
|
dc.subject |
ESCHERICHIA-COLI |
|
dc.subject |
CELL-CYCLE |
|
dc.subject |
0601 Biochemistry and Cell Biology |
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dc.subject |
Biomedical |
|
dc.subject |
Basic Science |
|
dc.subject |
02 Physical Sciences |
|
dc.subject |
06 Biological Sciences |
|
dc.title |
Characterization of the ubiquitin-specific protease activity of the mouse/human Unp/Unph oncoprotein. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1016/s0167-4838(00)00134-5 |
|
pubs.issue |
2 |
|
pubs.begin-page |
297 |
|
pubs.volume |
1481 |
|
dc.date.updated |
2022-06-16T04:30:44Z |
|
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
11018721 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/11018721 |
|
pubs.end-page |
309 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Research Support, Non-U.S. Gov't |
|
pubs.subtype |
Journal Article |
|
pubs.elements-id |
57416 |
|
pubs.org-id |
Medical and Health Sciences |
|
pubs.org-id |
School of Medicine |
|
pubs.org-id |
Paediatrics Child & Youth Hlth |
|
dc.identifier.eissn |
1878-2434 |
|
dc.identifier.pii |
S0167483800001345 |
|
pubs.record-created-at-source-date |
2022-06-16 |
|
pubs.online-publication-date |
2000-09 |
|