ArticlePlant molecular biology1998
Engineering in vivo instability of firefly luciferase and Escherichia coli beta-glucuronidase in higher plants using recognition elements from the ubiquitin pathway.
Article in Plant molecular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 49 citations in OpenAlex.
- Functional Divergence of the Arg/N-Degron Pathway Between the CropPlant direct · 2026Article
- BIG enhances Arg/N-degron pathway-mediated protein degradation to regulate Arabidopsis hypoxia responses and suberin deposition.The Plant cell · 2024Article
- Protocols for Studying Protein Stability in an Arabidopsis Protoplast Transient Expression System.Methods in molecular biology (Clifton, N.J.) · 2023Article
- A simple and efficientPlant direct · 2020Article
- The ubiquitination machinery of the ubiquitin system.The arabidopsis book · 2014Article
- The ubiquitin-proteasome system regulates the accumulation of Turnip yellow mosaic virus RNA-dependent RNA polymerase during viral infection.The Plant cell · 2010Article
- The N-end rule pathway controls multiple functions during Arabidopsis shoot and leaf development.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Use of mRNA- and protein-destabilizing elements to develop a highly responsive reporter system.Nucleic acids research · 2005Article
- Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features.Plant physiology · 2005Article
- Conserved ERAD-like quality control of a plant polytopic membrane protein.The Plant cell · 2005Article
- PRT1 of Arabidopsis is a ubiquitin protein ligase of the plant N-end rule pathway with specificity for aromatic amino-terminal residues.Plant physiology · 2003Article
- Rapid degradation of auxin/indoleacetic acid proteins requires conserved amino acids of domain II and is proteasome dependent.The Plant cell · 2001Article
- Use of ubiquitin fusions to augment protein expression in transgenic plants.Plant physiology · 1999Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ubiquitin pathway targets proteins for degradation through the post-translational covalent attachment of the 76 amino acid protein ubiquitin to epsilon-amino lysyl groups on substrate proteins. Two instability determinants recognized by the ubiquitin pathway in Saccharomyces cerevisiae have been identified. One is described by the N-end rule and requires specific destabilizing residues at the substrate protein N-termini along with a proximal lysyl residue for ubiquitin conjugation. The second is a linear uncleavable N-terminal ubiquitin moiety. The ability of these two determinants to function in higher plants was investigated in tobacco protoplast transient transfection assays using DNA encoding variants of well characterized reporter enzymes as substrates: firefly luciferase that is localized to peroxisomes (pxLUC), a cytosolic version of LUC (cLUC), and Escherichia coli beta-glucuronidase (GUS). cLUC with phenylalanine encoded at its mature N-terminus was 10-fold less abundant than cLUC with methionine at its mature N-terminus. GUS with phenylalanine encoded at its mature N-terminus was 3-fold less abundant than GUS with methionine at its mature N-terminus. The presence of a uncleavable N-terminal ubiquitin fusion resulted in 50-fold lower protein accumulation of cLUC, but had no effect on GUS. Both instability determinants had a much larger effect on cLUC than on pxLUC, suggesting that these degradation signals are either unrecognized or poorly recognized in the peroxisomes.
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