Identification and molecular properties of SUMO-binding proteins in arabidopsis

Handle URI:
http://hdl.handle.net/10754/561778
Title:
Identification and molecular properties of SUMO-binding proteins in arabidopsis
Authors:
Park, Hyeongcheol; Choi, Wonkyun; Park, Heejin; Cheong, Misun; Koo, Yoonduck; Shin, Gilok; Chung, Woosik; Kim, Woeyeon; Kim, Mingab; Bressan, Ray Anthony; Bohnert, Hans Jürgen; Lee, Sangyeol; Yun, Daejin
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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Publisher:
Springer Nature
Journal:
Molecules and Cells
Issue Date:
20-May-2011
DOI:
10.1007/s10059-011-2297-3
PubMed ID:
21607647
PubMed Central ID:
PMC3887670
Type:
Article
ISSN:
10168478
Sponsors:
We 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.
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887670
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorPark, Hyeongcheolen
dc.contributor.authorChoi, Wonkyunen
dc.contributor.authorPark, Heejinen
dc.contributor.authorCheong, Misunen
dc.contributor.authorKoo, Yoonducken
dc.contributor.authorShin, Giloken
dc.contributor.authorChung, Woosiken
dc.contributor.authorKim, Woeyeonen
dc.contributor.authorKim, Mingaben
dc.contributor.authorBressan, Ray Anthonyen
dc.contributor.authorBohnert, Hans Jürgenen
dc.contributor.authorLee, Sangyeolen
dc.contributor.authorYun, Daejinen
dc.date.accessioned2015-08-03T09:04:23Zen
dc.date.available2015-08-03T09:04:23Zen
dc.date.issued2011-05-20en
dc.identifier.issn10168478en
dc.identifier.pmid21607647en
dc.identifier.doi10.1007/s10059-011-2297-3en
dc.identifier.urihttp://hdl.handle.net/10754/561778en
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.en
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.en
dc.publisherSpringer Natureen
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887670en
dc.subjectArabidopsisen
dc.subjectMass spectrometryen
dc.subjectProteomicsen
dc.subjectSUMO binding proteinsen
dc.subjectSumoylationen
dc.titleIdentification and molecular properties of SUMO-binding proteins in arabidopsisen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalMolecules and Cellsen
dc.identifier.pmcidPMC3887670en
dc.contributor.institutionDivision of Applied Life Science , and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju 660-701, South Koreaen
dc.contributor.institutionDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN, United Statesen
dc.contributor.institutionBio-Crops Development Division, Department of Agricultural Biotechnology, National Academy of Agricultural Science, Suwon 441-707, South Koreaen
dc.contributor.institutionDepartments of Plant Biology and of Crop Sciences, University of Illinois at Urbana-Champaign, Urbana, United Statesen
kaust.authorBressan, Ray Anthonyen
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