Identification and molecular properties of SUMO-binding proteins in arabidopsis

Hyeongcheol Park, Wonkyun Choi, Heejin Park, Misun Cheong, Yoonduck Koo, Gilok Shin, Woosik Chung, Woeyeon Kim, Mingab Kim, Ray Anthony Bressan, Hans Jürgen Bohnert, Sangyeol Lee, Daejin Yun

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

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 detected 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 SUMO1ΔGG or AtSUMO3. The results suggest specific interactions between sumoylation targets and particular sumoylation enzymes. ©2011 KSMCB.
Original languageEnglish (US)
Pages (from-to)143-151
Number of pages9
JournalMolecules and Cells
Volume32
Issue number2
DOIs
StatePublished - May 20 2011

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

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