Numerous posttranslational modifications provide opportunities for the intricate regulation of metabolic enzymes at multiple levels.
The metabolic plasticity displayed by plants during normal development, and in response to environmental fluctuations and stressors, is essential for their growth and survival. The capacity to regulate metabolic enzymes intricately arises in part from posttranslational modifications that can affect enzymatic activity, intracellular localization, protein-protein interactions, and stability. Protein phosphorylation and thiol/disulfide redox modulation are important modifications in plants, and it is likely that O-glycosylation and S-nitrosylation will also emerge as important mechanisms. Recent advances in the field of proteomics, in particular the development of novel and specific chemistries for the detection of a diverse number of modifications, are rapidly expanding our awareness of possible modifications and our understanding of the enzymes whose functions are likely to be regulated posttranslationally.
Huber
Steven C
SC
United States Department of Agriculture-Agricultural Research Service, Photosynthesis Research Unit and Department of Plant Biology, University of Illinois, Urbana, Illinois 61801, USA. schuber1@life.uiuc.edu
Hardin
Shane C
SC
D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism; D006031:Glycosylation; D010084:Oxidation-Reduction; D010766:Phosphorylation; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D040901:Proteomics; D012694:Serine / Q000378:metabolism; D013879:Thioredoxins / Q000378:metabolism; D013912:Threonine / Q000378:metabolism
D010940:Plant Proteins; D013912:Threonine; D012694:Serine; D013879:Thioredoxins; D003545:Cysteine