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KMID : 0578320110320020143
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Molecules and Cells
2011 Volume.32 No. 2 p.143 ~ p.151
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Identification and Molecular Properties of SUMO-Binding Proteins in Arabidopsis
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Park Hyeong-Cheol
Choi Won-Kyun
Park Hee-Jin
Cheong Mi-Sun
Koo Yoon-Duck
Shin Gil-Ok
Chung Woo-Sik
Kim Woe-Yeon
Kim Min-Gab
Ray A. Bressan
Hans J. Bohnert
Lee Sang-Yeol
Yun Dae-Jin
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Abstract
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Reversible conjugation of the small ubiquitin modifier (SUMO) peptide to proteins (SUMOylation) plays important roles in cellular processes in animals and yeasts. However, little is known about plant SUMO targets. To identify SUMO substrates in Arabidopsis and to probe for biological functions of SUMO proteins, we constructed 6xHis-3xFLAG fused AtSUMO1 (HFAtSUMO1) controlled by the CaMV35S promoter for transformation into Arabidopsis Col-0. After heat treatment, an increased sumoylation pattern was de-tected in the transgenic plants. SUMO1-modified proteins were selected after two-dimensional gel electrophoresis (2-DE) image analysis and identified using matrix-assisted laser-desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). We identified 27 proteins involved in a variety of processes such as nucleic acid metabolism, signaling, metabolism, and including proteins of unknown functions. Binding and sumoylation patterns were confirmed independently. Surprisingly, MCM3 (At5G46280), a DNA replication licensing factor, only interacted with and became sumoylated by AtSUMO1, but not by SUMO1?GG or AtSUMO3. The results suggest specific interactions between sumoylation targets and particular sumoylation enzymes.
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KEYWORD
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Arabidopsis, mass spectrometry, proteomics, SUMO binding proteins, Sumoylation
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