Source:http://linkedlifedata.com/resource/pubmed/id/20561251
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
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| pubmed:dateCreated |
2010-10-22
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| pubmed:abstractText |
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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Abscisic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Small Ubiquitin-Related Modifier...,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
1365-3040
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| pubmed:author |
pubmed-author:BaekDongwonD,
pubmed-author:BohnertHans JHJ,
pubmed-author:BressanRay ARA,
pubmed-author:CheongMi SunMS,
pubmed-author:ChungWoo SikWS,
pubmed-author:HongHyewonH,
pubmed-author:KimDoh HoonDH,
pubmed-author:KooSung CheolSC,
pubmed-author:KuoH CHC,
pubmed-author:LeeSang YeolSY,
pubmed-author:ParkHee JinHJ,
pubmed-author:ParkHyeong CheolHC,
pubmed-author:YunDae-JinDJ
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| pubmed:copyrightInfo |
© 2010 Blackwell Publishing Ltd.
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| pubmed:issnType |
Electronic
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| pubmed:volume |
33
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1923-34
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| pubmed:meshHeading |
pubmed-meshheading:20561251-Abscisic Acid,
pubmed-meshheading:20561251-Amino Acid Sequence,
pubmed-meshheading:20561251-Arabidopsis,
pubmed-meshheading:20561251-Cell Nucleus,
pubmed-meshheading:20561251-Gene Expression Regulation, Plant,
pubmed-meshheading:20561251-Genetic Complementation Test,
pubmed-meshheading:20561251-Hot Temperature,
pubmed-meshheading:20561251-Molecular Sequence Data,
pubmed-meshheading:20561251-Oryza sativa,
pubmed-meshheading:20561251-Plant Proteins,
pubmed-meshheading:20561251-Plants, Genetically Modified,
pubmed-meshheading:20561251-RNA, Plant,
pubmed-meshheading:20561251-Sequence Homology, Amino Acid,
pubmed-meshheading:20561251-Small Ubiquitin-Related Modifier Proteins,
pubmed-meshheading:20561251-Stress, Physiological,
pubmed-meshheading:20561251-Sumoylation,
pubmed-meshheading:20561251-Tobacco,
pubmed-meshheading:20561251-Ubiquitin-Protein Ligases
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| pubmed:year |
2010
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| pubmed:articleTitle |
Functional characterization of the SIZ/PIAS-type SUMO E3 ligases, OsSIZ1 and OsSIZ2 in rice.
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| pubmed:affiliation |
Division of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center and Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju 660-701, Korea. hcpark@gnu.ac.kr
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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