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The progress on The Ubiquitin 26S Proteasome Pathway in Plants |
huang hai-jie |
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Abstract Selective protein degradation by the ubiquitin 26S proteasome pathway has emerged as a key regulatory mechanism in a wide variety of cellular processes. The ubiquitin/26S proteosome pathway mainly consists of ubiquitin activating enzyme (E1),ubiquitin conjugating enzyme (E2),ubiquitin protein ligase (E3), and 26S proteasome. In an ATP-dependent reaction,uibquitin (Ub) is conjugated to E1,the activated Ub is then transferred to an E2. Finally,the Ub-E2 intermediate delivers the Ub to the target protein by E3 recognition. Polyubiquinated proteins are eventually degraded by the 26S proteasome.In plants,regulated protein degradation by /26S proteasome pathway contributes significantly to development by affecting a wide range of progress, including hormone signaling, photomorphogenesis, self- incompatibility and cell cycle.This review highlights the recent progress towards understanding the role of the Ub/26S proteasome pathway during plant development.
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Received: 20 February 2008
Published: 25 July 2008
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