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Methods Mol Biol. 2009;479:147-71. doi: 10.1007/978-1-59745-289-2_10.

Examining protein stability and its relevance for plant growth and development.

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Department of Developmental Genetics, Center for Plant Molecular Biology, Tübingen University, Tübingen, Germany.


Eukaryotes control many aspects of growth and development such as cell cycle progression and gene expression through the selective degradation of regulatory proteins by way of the 26S proteasome. Generally, proteasomal degradation requires the poly-ubiquitylation of degradation targets by E1 ubiquitin activating enzymes, E2 ubiquitin conjugating enzymes, and E3 ubiquitin ligases. Specificity is brought to the process by E3 ubiquitin ligases, which engage in direct interactions with the degradation substrate to bring it into the proximity of the E2 enzyme. The abundance of genes encoding E3 ligase subunits in plant genomes invites the hypothesis that protein degradation plays an important role in the control of many plant growth processes, and it is therefore not surprising that proteasomal degradation has already been implicated in several important response pathways. However, most of the genes with a predicted role in the ubiquitin-proteasome pathway still remain to be characterized and the identity of their degradation substrates needs to be revealed. In this chapter, we give an overview of the ubiquitin-proteasome system and the pathway proteins that have been examined in Arabidopsis to date. We review the methods required to identify and characterize the proteins that play a role in protein degradation or that are the target for proteasomal degradation.

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