Functional characterization of the SIZ/PIAS-type SUMO E3 ligases, OsSIZ1 and OsSIZ2 in rice

Handle URI:
http://hdl.handle.net/10754/561553
Title:
Functional characterization of the SIZ/PIAS-type SUMO E3 ligases, OsSIZ1 and OsSIZ2 in rice
Authors:
Park, Hyeongcheol; Kim, Hun; Koo, Sungcheol; Park, Heejin; Cheong, Misun; Hong, Hyewon; Baek, Dongwon; Chung, Woosik; Kim, Dohhoon; Bressan, Ray Anthony; Lee, Sangyeol; Bohnert, Hans Jürgen; Yun, Daejin
Abstract:
Sumoylation is a post-translational regulatory process in diverse cellular processes in eukaryotes, involving conjugation/deconjugation of small ubiquitin-like modifier (SUMO) proteins to other proteins thus modifying their function. The PIAS [protein inhibitor of activated signal transducers and activators of transcription (STAT)] and SAP (scaffold attachment factor A/B/acinus/PIAS)/MIZ (SIZ) proteins exhibit SUMO E3-ligase activity that facilitates the conjugation of SUMO proteins to target substrates. Here, we report the isolation and molecular characterization of Oryza sativa SIZ1 (OsSIZ1) and SIZ2 (OsSIZ2), rice homologs of Arabidopsis SIZ1. The rice SIZ proteins are localized to the nucleus and showed sumoylation activities in a tobacco system. Our analysis showed increased amounts of SUMO conjugates associated with environmental stresses such as high and low temperature, NaCl and abscisic acid (ABA) in rice plants. The expression of OsSIZ1 and OsSIZ2 in siz1-2 Arabidopsis plants partially complemented the morphological mutant phenotype and enhanced levels of SUMO conjugates under heat shock conditions. In addition, ABA-hypersensitivity of siz1-2 seed germination was partially suppressed by OsSIZ1 and OsSIZ2. The results suggest that rice SIZ1 and SIZ2 are able to functionally complement Arabidopsis SIZ1 in the SUMO conjugation pathway. Their effects on the Arabidopsis mutant suggest a function for these genes related to stress responses and stress adaptation. © 2010 Blackwell Publishing Ltd.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Publisher:
Wiley-Blackwell
Journal:
Plant, Cell & Environment
Issue Date:
18-Jun-2010
DOI:
10.1111/j.1365-3040.2010.02195.x
PubMed ID:
20561251
Type:
Article
ISSN:
01407791
Sponsors:
This work was supported by grants from the Biogreen 21 Program (20080401034023) of the Rural Development Administration, the World Class University Program (R32-10148) and the Environmental Biotechnology National Core Research Center (Grant#: R15-2003-012-01002-00) funded by the Ministry of Education, Science and Technology in Korea.
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorPark, Hyeongcheolen
dc.contributor.authorKim, Hunen
dc.contributor.authorKoo, Sungcheolen
dc.contributor.authorPark, Heejinen
dc.contributor.authorCheong, Misunen
dc.contributor.authorHong, Hyewonen
dc.contributor.authorBaek, Dongwonen
dc.contributor.authorChung, Woosiken
dc.contributor.authorKim, Dohhoonen
dc.contributor.authorBressan, Ray Anthonyen
dc.contributor.authorLee, Sangyeolen
dc.contributor.authorBohnert, Hans Jürgenen
dc.contributor.authorYun, Daejinen
dc.date.accessioned2015-08-02T09:14:04Zen
dc.date.available2015-08-02T09:14:04Zen
dc.date.issued2010-06-18en
dc.identifier.issn01407791en
dc.identifier.pmid20561251en
dc.identifier.doi10.1111/j.1365-3040.2010.02195.xen
dc.identifier.urihttp://hdl.handle.net/10754/561553en
dc.description.abstractSumoylation is a post-translational regulatory process in diverse cellular processes in eukaryotes, involving conjugation/deconjugation of small ubiquitin-like modifier (SUMO) proteins to other proteins thus modifying their function. The PIAS [protein inhibitor of activated signal transducers and activators of transcription (STAT)] and SAP (scaffold attachment factor A/B/acinus/PIAS)/MIZ (SIZ) proteins exhibit SUMO E3-ligase activity that facilitates the conjugation of SUMO proteins to target substrates. Here, we report the isolation and molecular characterization of Oryza sativa SIZ1 (OsSIZ1) and SIZ2 (OsSIZ2), rice homologs of Arabidopsis SIZ1. The rice SIZ proteins are localized to the nucleus and showed sumoylation activities in a tobacco system. Our analysis showed increased amounts of SUMO conjugates associated with environmental stresses such as high and low temperature, NaCl and abscisic acid (ABA) in rice plants. The expression of OsSIZ1 and OsSIZ2 in siz1-2 Arabidopsis plants partially complemented the morphological mutant phenotype and enhanced levels of SUMO conjugates under heat shock conditions. In addition, ABA-hypersensitivity of siz1-2 seed germination was partially suppressed by OsSIZ1 and OsSIZ2. The results suggest that rice SIZ1 and SIZ2 are able to functionally complement Arabidopsis SIZ1 in the SUMO conjugation pathway. Their effects on the Arabidopsis mutant suggest a function for these genes related to stress responses and stress adaptation. © 2010 Blackwell Publishing Ltd.en
dc.description.sponsorshipThis work was supported by grants from the Biogreen 21 Program (20080401034023) of the Rural Development Administration, the World Class University Program (R32-10148) and the Environmental Biotechnology National Core Research Center (Grant#: R15-2003-012-01002-00) funded by the Ministry of Education, Science and Technology in Korea.en
dc.publisherWiley-Blackwellen
dc.subjectOryza sativaen
dc.subjectSIZ/PIAS-type SUMO E3-ligaseen
dc.subjectStress responseen
dc.subjectSUMOen
dc.subjectSumoylationen
dc.titleFunctional characterization of the SIZ/PIAS-type SUMO E3 ligases, OsSIZ1 and OsSIZ2 in riceen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalPlant, Cell & Environmenten
dc.contributor.institutionDivision of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center, Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju, 660-701, South Koreaen
dc.contributor.institutionCollege of Natural Resources and Life Science, Dong-A University, Busan, 604-714, South Koreaen
dc.contributor.institutionDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN, 47907-2054, United Statesen
dc.contributor.institutionDepartments of Plant Biology and of Crop Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United Statesen
kaust.authorBressan, Ray Anthonyen

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