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Author Kim, Do-Young ♦ Scalf, Mark ♦ Smith, Lloyd M. ♦ Vierstra, Richard D.
Source World Health Organization (WHO)-Global Index Medicus
Content type Text
Publisher American Society of Plant Biologists
File Format HTM / HTML
Language English
Difficulty Level Medium
Subject Domain (in DDC) Natural sciences & mathematics ♦ Chemistry & allied sciences ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Natural history of organisms ♦ Technology ♦ Medicine & health ♦ Human physiology ♦ Pharmacology and therapeutics ♦ Diseases ♦ Manufacture for specific uses ♦ Precision instruments & other devices
Subject Domain (in MeSH) Eukaryota ♦ Organisms ♦ Macromolecular Substances ♦ Amino Acids, Peptides, and Proteins ♦ Chemical Actions and Uses ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment ♦ Chemical Phenomena ♦ Biological Sciences ♦ Natural Science Disciplines ♦ Physical Sciences
Subject Keyword Discipline Botany ♦ Arabidopsis Proteins ♦ Metabolism ♦ Arabidopsis ♦ Proteome ♦ Proteomics ♦ Methods ♦ Ubiquitinated Proteins ♦ Amino Acid Sequence ♦ Genetics ♦ Growth & Development ♦ Cysteine Proteinase Inhibitors ♦ Pharmacology ♦ Immunoblotting ♦ Leupeptins ♦ Lysine ♦ Mass Spectrometry ♦ Plants, Genetically Modified ♦ Proteasome Endopeptidase Complex ♦ Ubiquitin ♦ Classification ♦ Ubiquitination ♦ Drug Effects ♦ Journal Article ♦ Research Support, N.i.h., Extramural ♦ Research Support, Non-u.s. Gov't
Abstract The posttranslational addition of ubiquitin (Ub) profoundly controls the half-life, interactions, and/or trafficking of numerous intracellular proteins. Using stringent two-step affinity methods to purify Ub-protein conjugates followed by high-sensitivity mass spectrometry, we identified almost 950 ubiquitylation substrates in whole Arabidopsis thaliana seedlings. The list includes key factors regulating a wide range of biological processes, including metabolism, cellular transport, signal transduction, transcription, RNA biology, translation, and proteolysis. The ubiquitylation state of more than half of the targets increased after treating seedlings with the proteasome inhibitor MG132 (carbobenzoxy-Leu-Leu-Leu-al), strongly suggesting that Ub addition commits many to degradation by the 26S proteasome. Ub-attachment sites were resolved for a number of targets, including six of the seven Lys residues on Ub itself with a Lys-48>Lys-63>Lys-11>>>Lys-33/Lys-29/Lys-6 preference. However, little sequence consensus was detected among conjugation sites, indicating that the local environment has little influence on global ubiquitylation. Intriguingly, the level of Lys-11-linked Ub polymers increased substantially upon MG132 treatment, revealing that they might be important signals for proteasomal breakdown. Taken together, this proteomic analysis illustrates the breadth of plant processes affected by ubiquitylation and provides a deep data set of individual targets from which to explore the roles of Ub in various physiological and developmental pathways.
Description Country affiliation: United States
Author Affiliation: Kim DY ( Department of Genetics, University of Wisconsin, Madison, Wisconsin 53706, USA.)
ISSN 10404651
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Reading ♦ Research ♦ Self Learning
Interactivity Type Expositive
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2013-05-01
Publisher Place United States
e-ISSN 1531298X
Journal THE PLANT CELL ONLINE
Volume Number 25
Issue Number 5


Source: WHO-Global Index Medicus