Document Detail

SUMO and SUMOylation in plants.
MedLine Citation:
PMID:  21912873     Owner:  NLM     Status:  MEDLINE    
The traditional focus on the central dogma of molecular biology, from gene through RNA to protein, has now been replaced by the recognition of an additional mechanism.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 biotic stressses, as well 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 been done lately in plants. Further SUMO noncovalent binding appears to have function in other model organisms and SUMO interacting proteins in plants will be of interest to plant biologists who dissect the dynamic function of SUMO. This review will discuss results of recent insights into the role of sumoylation in plants.
Hee Jin Park; Woe-Yeon Kim; Hyeong Cheol Park; Sang Yeol Lee; Hans J Bohnert; Dae-Jin Yun
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2011-09-09
Journal Detail:
Title:  Molecules and cells     Volume:  32     ISSN:  0219-1032     ISO Abbreviation:  Mol. Cells     Publication Date:  2011 Oct 
Date Detail:
Created Date:  2011-10-31     Completed Date:  2012-03-16     Revised Date:  2014-02-21    
Medline Journal Info:
Nlm Unique ID:  9610936     Medline TA:  Mol Cells     Country:  United States    
Other Details:
Languages:  eng     Pagination:  305-16     Citation Subset:  IM    
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MeSH Terms
Environmental Exposure / adverse effects
Plant Physiological Processes
Protein Processing, Post-Translational
Small Ubiquitin-Related Modifier Proteins / physiology*
Stress, Physiological
Ubiquitin / metabolism
Reg. No./Substance:
0/Small Ubiquitin-Related Modifier Proteins; 0/Ubiquitin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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