RT Journal Article
SR Electronic
T1 Detecting and Measuring Cotranslational Protein Degradation in Vivo
JF Science
JO Science
FD American Association for the Advancement of Science
SP 2117
OP 2120
DO 10.1126/science.289.5487.2117
VO 289
IS 5487
A1 Turner, Glenn C.
A1 Varshavsky, Alexander
YR 2000
UL http://science.sciencemag.org/content/289/5487/2117.abstract
AB 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.