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Detecting and Measuring Cotranslational Protein Degradation in Vivo

Turner, Glenn C. and Varshavsky, Alexander (2000) Detecting and Measuring Cotranslational Protein Degradation in Vivo. Science, 289 (5487). pp. 2117-2120. ISSN 0036-8075. doi:10.1126/science.289.5487.2117.

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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.

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Varshavsky, Alexander0000-0002-4011-258X
Additional Information:© 2000 American Association for the Advancement of Science. Received 15 March 2000; accepted 31 July 2000. We thank F. Lévy and N. Johnsson for their contributions to early stages of this work and R. Deshaies, T. Iverson, T.-M. Yi, and members of the Varshavsky laboratory for helpful discussions and comments on the manuscript. This study was supported by a grant to A.V. from NIH. G.T. was supported in part by Amgen.
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Issue or Number:5487
Record Number:CaltechAUTHORS:20141112-112135305
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:51655
Deposited By: Tony Diaz
Deposited On:12 Nov 2014 21:33
Last Modified:10 Nov 2021 19:13

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