Abstract
Although sucrose availability is crucial for commitment to plant cell division during G1 phase, it has remained uncertain how protein levels of core cell cycle genes are regulated. We found that Arabidopsis retinoblastoma-related protein1 (AtRBR1) and three E2F proteins were degraded under limited sucrose conditions, while protein abundance increased in response to treatment with the proteasome inhibitor MG132. We conclude that Arabidopsis key cell cycle proteins are degraded in a proteasome-dependent manner during sucrose starvation in Arabidopsis suspension MM2d cells.
Copyright © 2011 Elsevier Masson SAS. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Arabidopsis / metabolism*
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Arabidopsis Proteins / metabolism*
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Cell Cycle Proteins / metabolism*
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Cells, Cultured
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Cysteine Proteinase Inhibitors / pharmacology
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E2F Transcription Factors / metabolism
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G1 Phase*
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Gene Expression Regulation, Plant
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Leupeptins / pharmacology
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Proteasome Endopeptidase Complex / metabolism*
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Starvation
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Sucrose / metabolism*
Substances
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Arabidopsis Proteins
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Cell Cycle Proteins
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Cysteine Proteinase Inhibitors
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E2F Transcription Factors
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Leupeptins
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RBR1 protein, Arabidopsis
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Sucrose
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Proteasome Endopeptidase Complex
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benzyloxycarbonylleucyl-leucyl-leucine aldehyde