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A test of fusion protein stability in the plant Arabidopsis thaliana reveals degradation signals from ACC synthase and from the plant N-end rule pathway

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Schlogelhofer,  P.
Dept. of Plant Developmental Biology (George Coupland), MPI for Plant Breeding Research, Max Planck Society;

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Bachmair,  A.
Dept. of Plant Developmental Biology (George Coupland), MPI for Plant Breeding Research, Max Planck Society;

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Schlogelhofer, P., & Bachmair, A. (2002). A test of fusion protein stability in the plant Arabidopsis thaliana reveals degradation signals from ACC synthase and from the plant N-end rule pathway. Plant Cell Reports, 21(2), 174-179.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-3DA0-F
Abstract
We tested three different protein domains for their ability to confer a short half life onto the otherwise stable test protein dihydrofolate reductase (DHFR) in the plant Arabidopsis thaliana. E-DHFR, a protein with Glu as the first residue, is metabolically unstable in Arabidopsis, indicating that Glu is a destabilizing residue of the plant N-end rule pathway. In contrast, the degradation signal deg1 from Saccharomyces cerevisiae transcription factor Matalpha2p is not recognized when present at the amino-terminus of DHFR. Finally, we show that the amino-terminal 93 amino acids of the plant protein 1- aminocyclopropane-1-carboxylic acid synthase contain a degradation signal that is also active in yeast.