NDLI: Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome.

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Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome.

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Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Inada, Toshifumi Kuroha, Kazushige Tatematsu, Tsuyako Dimitrova, Lyudmila N.
Description	Author Affiliation: Dimitrova LN ( Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.)
Abstract	The potentially deleterious effects of aberrant mRNA lacking a termination codon (nonstop mRNA) are ameliorated by translation arrest, proteasome-mediated protein destabilization, and rapid mRNA degradation. Because polylysine synthesis via translation of the poly(A) mRNA tail leads to translation arrest and protein degradation by the proteasome, we examined the effects of other amino acid sequences. Insertion of 12 consecutive basic amino acids between GFP and HIS3 reporter genes, but not a stem-loop structure, resulted in degradation of the truncated green fluorescent protein (GFP) products by the proteasome. Translation arrest products derived from GFP-R12-FLAG-HIS3 or GFP-K12-FLAG-HIS3 mRNA were detected in a not4Delta mutant, and MG132 treatment did not affect the levels of the truncated arrest products. Deletion of other components of the Ccr4-Not complex did not increase the levels of the translation arrest products or reporter mRNAs. A L35A substitution in the Not4p RING finger domain, which disrupted its interaction with the Ubc4/Ubc5 E2 enzyme and its activity as an ubiquitin-protein ligase, also abrogated the degradation of arrest products. These results suggest that Not4p, a component of the Ccr4-Not complex, may act as an E3 ubiquitin-protein ligase for translation arrest products. The results let us propose that the interaction between basic amino acid residues and the negatively charged exit tunnel of the ribosome leads to translation arrest followed by Not4p-mediated ubiquitination and protein degradation by the proteasome.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	16
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-04-17
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Gene Expression Regulation Peptides Metabolism Proteasome Endopeptidase Complex Protein Biosynthesis Ubiquitin-Protein Ligases Amino Acid Sequence Molecular Sequence Data Genetics Recombinant Fusion Proteins Repressor Proteins Ribosomes Saccharomyces Cerevisiae Saccharomyces Cerevisiae Proteins Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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