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Plant Development: Regulation by Protein Degradation

Many aspects of eukaryotic development depend on regulated protein degradation by the ubiquitin-proteasome pathway. This highly conserved pathway promotes covalent attachment of ubiquitin to protein substrates through the sequential action of three enzymes called a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin-protein ligase (E3). Most ubiquitinated proteins are then targeted for degradation by the 26S proteasome. Recent studies have also shown that the ubiquitin-related protein RUB/Nedd8 and the proteasome-related COP9 signalosome complex cooperate with the ubiquitin-proteasome pathway to promote protein degradation. Most of these components are conserved in all three eukaryotic kingdoms. However, the known targets of the pathway in plants, and the developmental processes they regulate, are specific to the plant kingdom.

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Resource Type: Journal article/Issue, Illustration
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16, Graduate, Continuing education

Author and Copyright


Authors and Editors: Hanjo Hellmann of Molecular Cell and Developmental Biology, University of Texas, Mark Estelle of Molecular Cell and Developmental Biology, University of Texas
Publisher: AAAS
Format: text/html
Copyright and other restrictions: Yes
Cost: No

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American Association for the Advancement of Science


     
   

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