Article
Structure and function of the yeast listerin (Ltn1) conserved N-terminal domain in binding to stalled 60S ribosomal subunits.
Proceedings of the National Academy of Sciences of the United States of America - 19 Jul 2016
Doamekpor Selom K, Lee Joong-Won, Hepowit Nathaniel L, Wu Cheng, Charenton Clement, Leonard Marilyn, Bengtson Mario H, Rajashankar Kanagalaghatta R, Sachs Matthew S, Lima Christopher D, Joazeiro Claudio A P
Abstract excerpt
The Ltn1 E3 ligase (listerin in mammals) has emerged as a paradigm for understanding ribosome-associated ubiquitylation. Ltn1 binds to 60S ribosomal subunits to ubiquitylate nascent polypeptides that become stalled during synthesis; among Ltn1's substrates are aberrant products of mRNA lacking stop codons [nonstop translation products (NSPs)]. Here, we report the reconstitution of NSP ubiquitylation in Neurospora...
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