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dc.contributor.authorPark, Hyeongcheol
dc.contributor.authorChoi, Wonkyun
dc.contributor.authorPark, Heejin
dc.contributor.authorCheong, Misun
dc.contributor.authorKoo, Yoonduck
dc.contributor.authorShin, Gilok
dc.contributor.authorChung, Woosik
dc.contributor.authorKim, Woeyeon
dc.contributor.authorKim, Mingab
dc.contributor.authorBressan, Ray Anthony
dc.contributor.authorBohnert, Hans Jürgen
dc.contributor.authorLee, Sangyeol
dc.contributor.authorYun, Daejin
dc.date.accessioned2015-08-03T09:04:23Z
dc.date.available2015-08-03T09:04:23Z
dc.date.issued2011-05-20
dc.identifier.citationPark, H. C., Choi, W., Park, H. J., Cheong, M. S., Koo, Y. D., Shin, G., … Yun, D.-J. (2011). Identification and molecular properties of SUMO-binding proteins in Arabidopsis. Molecules and Cells, 32(2), 143–151. doi:10.1007/s10059-011-2297-3
dc.identifier.issn10168478
dc.identifier.pmid21607647
dc.identifier.doi10.1007/s10059-011-2297-3
dc.identifier.urihttp://hdl.handle.net/10754/561778
dc.description.abstractReversible 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.
dc.description.sponsorshipWe thank Dr. Jian-Min Zhou for providing the NLuc and CLuc plasmids and Dr. Katsunori Tanaka for providing the pCDFDuet-AtSUMO-AtSCE1, pACYCDuet-AtSAEb-AtSAE2, and pET28a-AtMYB30 plasmids. This work was supported by grants from the Biogreen 21 Program (grant No. PJ006654) of the Rural Development Administration, World Class University Program (R32-10148) funded by the Ministry of Education, Science and Technology in Korea, and the National Research Foundation of Korea Grant funded by the Korean Government (Ministry of Education, Science and Technology) [NRF-2010-359-F00006]. GS was supported by scholarship from the Brain Korea 21 program of the Ministry of Education, Science and Technology in Korea.
dc.publisherSpringer Science and Business Media LLC
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887670
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887670
dc.rightsArchived with thanks to Springer Science and Business Media LLC
dc.rightsThis file is an open access version redistributed from: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887670
dc.subjectArabidopsis
dc.subjectMass spectrometry
dc.subjectProteomics
dc.subjectSUMO binding proteins
dc.subjectSumoylation
dc.titleIdentification and molecular properties of SUMO-binding proteins in arabidopsis
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.identifier.journalMolecules and Cells
dc.identifier.pmcidPMC3887670
dc.rights.embargodate2012-05-20
dc.eprint.versionPost-print
dc.contributor.institutionDivision of Applied Life Science , and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju 660-701, South Korea
dc.contributor.institutionDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN, United States
dc.contributor.institutionBio-Crops Development Division, Department of Agricultural Biotechnology, National Academy of Agricultural Science, Suwon 441-707, South Korea
dc.contributor.institutionDepartments of Plant Biology and of Crop Sciences, University of Illinois at Urbana-Champaign, Urbana, United States
kaust.personBressan, Ray Anthony
refterms.dateFOA2021-06-23T06:34:24Z
dc.date.published-online2011-05-20
dc.date.published-print2011-08


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