Detecting and measuring cotranslational protein degradation in vivo

Turner, G. C., Varshavsky, A. (2000) Detecting and measuring cotranslational protein degradation in vivo. Science, 289 (5487). pp. 2117-2120. ISSN 00368075 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/11000112
DOI: 10.1126/science.289.5487.2117

Abstract

Nascent polypeptides emerging from the ribosome and not yet folded may at least transiently present degradation signals similar to those recognized by the ubiquitin system in misfolded proteins. The ubiquitin sandwich technique was used to detect and measure cotranslational protein degradation in living cells. More than 50 percent of nascent protein molecules bearing an amino-terminal degradation signal can be degraded cotranslationally, never reaching their mature size before their destruction by processive proteolysis. Thus, the folding of nascent proteins, including abnormal ones, may be in kinetic competition with pathways that target these proteins for degradation cotranslationally.

Item Type: Paper
Uncontrolled Keywords: article competitive inhibition in vivo study labeling index priority journal protein analysis protein degradation protein domain protein folding quality control RNA translation beta-Galactosidase Cysteine Endopeptidases DNA-Directed RNA Polymerases Endopeptidases Fungal Proteins Multienzyme Complexes Peptides Protein Structure, Tertiary Recombinant Fusion Proteins Saccharomyces cerevisiae Tetrahydrofolate Dehydrogenase Translation, Genetic Ubiquitins
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > ubiquitin ligase
CSHL Authors:
Communities: CSHL labs > Turner lab
Depositing User: CSHL Librarian
Date: 2000
Date Deposited: 11 Apr 2012 15:01
Last Modified: 14 Mar 2013 16:17
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26145

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