| Proteasome subunit zeta, a putative ribonuclease, is also found as a free monomer. | |
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MedLine Citation:
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PMID: 10363657 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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20 S Proteasomes are large proteinase complexes found in eukaryotic cells where they degrade cell proteins in an ATP-dependent manner. Proteasomes consist of 14 different subunits. One of them, zeta, was found in HeLa cells at a concentration of 890 microg per g of cell protein. A large proportion of zeta was found in the free state rather than incorporated into proteasomes, namely 28% in HeLa cells and 37% in BSC-1 cells. Free zeta was found in both nuclei and cytoplasm. In HeLa cells free zeta had a t1/2 of 2.8 h, compared to 5 d for proteasomes, and did not exchange with zeta in proteasomes. We confirmed (Petit F et al.: Biochem. J. 326: 93-98 (1997)) that both 20 S proteasomes and free zeta subunits possess RNase activity though the activities were very low: 4 mMoles and 0.6 mMoles of tobacco mosaic virus RNA degraded per mole of enzyme per min, respectively. The physiological function of the relatively abundant zeta monomers is not known. |
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Authors:
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L Jørgensen; K B Hendil |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecular biology reports Volume: 26 ISSN: 0301-4851 ISO Abbreviation: Mol. Biol. Rep. Publication Date: 1999 Apr |
Date Detail:
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Created Date: 1999-09-14 Completed Date: 1999-09-14 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0403234 Medline TA: Mol Biol Rep Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 119-23 Citation Subset: IM |
Affiliation:
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August Krogh Institute, Copenhagen O, Denmark. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Cysteine Endopeptidases
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chemistry*,
isolation & purification,
metabolism Electrophoresis, Polyacrylamide Gel Erythrocytes / enzymology Hela Cells Humans Multienzyme Complexes / chemistry*, isolation & purification, metabolism Proteasome Endopeptidase Complex Ribonucleases / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Multienzyme Complexes; EC 3.1.-/Ribonucleases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex |
| Comments/Corrections | |
Erratum In:
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Mol Biol Rep 1999 Aug;26(3):215-6 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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