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New insights into the role of the small ubiquitin-like modifier (SUMO) in plants.

Authors
  • Park, Hee Jin1
  • Yun, Dae-Jin
  • 1 Division of Applied Life Science (BK21 program), and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju, Gyeongsangnam-do, Korea. , (North Korea)
Type
Published Article
Journal
International review of cell and molecular biology
Publication Date
Jan 01, 2013
Volume
300
Pages
161–209
Identifiers
DOI: 10.1016/B978-0-12-405210-9.00005-9
PMID: 23273862
Source
Medline
License
Unknown

Abstract

Small ubiquitin-like modifier (SUMO) is a small (∼12kDa) protein that occurs in all eukaryotes and participates in the reversible posttranslational modification of target cellular proteins. The three-dimensional structure of SUMO and ubiquitin (Ub) are superimposable although there is very little similarity in their primary amino acid sequences. In all organisms, conjugation and deconjugation of Ub and SUMO proceed by the same reactions while using pathway-specific enzymes. SUMO conjugation in plants is a part of the controls governing important biological processes such as growth, development, flowering, environmental (abiotic) stress responses, and response to pathogen infection. Most of the evidence for this comes from genetic analyses. Recent efforts to dissect the function of sumoylation have focused on uncovering targets of SUMO conjugation by using either a yeast two-hybrid screen employing components of the SUMO cycle as bait or by using affinity purification of SUMO-conjugated proteins followed by identification of these proteins by mass spectrometry. This chapter reviews the current knowledge regarding sumoylation in plants, with special focus on the model plant Arabidopsis thaliana.

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