Affordable Access

Detecting and measuring cotranslational protein degradation in vivo

Authors
Publication Date
Keywords
  • Protein Structure
  • Function
  • Modification
  • Protein Characterization
  • Protein Structure Rendering
  • Ubiquitin Ligase
Disciplines
  • Biology

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.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Measuring in vivo intracellular protein degradatio...

on Journal of animal science April 2008

Measuring In Vivo Protein Half-Life

on Chemistry & Biology Jan 01, 2011

Coupling of cytosolic protein synthesis and mitoch...

on Journal of Biological Chemistr... Jan 25, 1993
More articles like this..