| SUMO and SUMOylation in plants. | |
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MedLine Citation:
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PMID: 21912873 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The traditional focus on the central dogma of molecular biology, from gene through RNA to protein, has now been replaced by the recognition of an additional mechanism. The new regulatory mechanism, post-translational modifications to proteins, can actively alter protein function or activity introducing additional levels of functional complexity by altering cellular and sub-cellular location, protein interactions and the outcome of biochemical reaction chains. Modifications by ubiquitin (Ub) and ubiquitin-like modifiers systems are conserved in all eukaryotic organisms. One of them, small ubiquitin-like modifier (SUMO) is present in plants. The SUMO mechanism includes several isoforms of proteins that are involved in reactions of sumoylation and de-sumoylation. Sumoylation affects several important processes in plants. Outstanding among those are responses to environmental stresses. These may be abiotic stresses, such as phosphate deficiency, heat, low temperature, and drought, or as well biotic stressses, including defense reactions to pathogen infection. Also, the regulations of flowering time, cell growth and development, and nitrogen assimilation have recently been added to this list. Identification of SUMO targets is material to characterize the function of sumoylation or desumoylation. Affinity purification and mass spectrometric identification have done lately in plants. Further SUMO non-covalent binding appears to have function in other model organisms and SUMO interacting proteins in plants will be interest of plant biologists who dissect the dynamic function of SUMO. This review will discuss results of recent insights into the role of sumoylation in plants. |
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Authors:
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Hee Jin Park; Woe-Yeon Kim; Hyeong Cheol Park; Sang Yeol Lee; Hans J Bohnert; Dae-Jin Yun |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-9-9 |
Journal Detail:
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Title: Molecules and cells Volume: - ISSN: 0219-1032 ISO Abbreviation: - Publication Date: 2011 Sep |
Date Detail:
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Created Date: 2011-9-13 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9610936 Medline TA: Mol Cells Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Division of Applied Life Science (Brain Korea 21 Program), and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju, 660-701, Korea. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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