Document Detail


Post-translational events and modifications regulating plant enzymes involved in isoprenoid precursor biosynthesis.
MedLine Citation:
PMID:  23415327     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Identification of regulatory enzymes is fundamental for engineering metabolic pathways such as the isoprenoid one. All too often, investigation of gene expression remains the major trend in unraveling regulation mechanisms of the isoprenoid cytosolic mevalonate and the plastid-localized methylerythritol phosphate metabolic pathways. But such metabolic regulatory enzymes are frequently multilevel-regulated, especially at a post-translational level. A prominent example is the endoplasmic reticulum-bound 3-hydroxy-3-methylglutaryl coenzyme A reductase catalyzing the synthesis of mevalonic acid. Despite the discovery and the intense efforts made to understand regulation of the methylerythritol phosphate pathway, this enzyme remains a leading player in the regulation of the whole isoprenoid pathway. Strict correlation between this enzyme's gene expression, protein level and enzyme activity is not observed, thus confirming multilevel-regulation. In this context, besides post-translational modifications of proteins, we have to consider feedback of metabolic flow and allosteric regulation, alternative protein structures, targeted proteolysis and/or redox regulation. Such multilevel-regulation processes deliver a range of benefits including rapid response to environmental and physiological challenges or metabolic fluctuations. This review specially emphasizes essential functions of these post-translational events that permit the close regulation of key enzymes involved in plant isoprenoid precursor biosynthesis.
Authors:
Andréa Hemmerlin
Related Documents :
18997407 - Cloning of the gene encoding alpha-methylserine hydroxymethyltransferase from aminobact...
11811537 - Glycerol metabolism in superoxide dismutase-deficient escherichia coli.
3291877 - The cloning and over-expression of paba synthase in e. coli.
8563147 - Overexpression and purification of non-glycosylated recombinant endo-beta-n-acetylgluco...
3458247 - Zero-order ultrasensitivity in the regulation of glycogen phosphorylase.
17303657 - The glucose-6-phosphate transporter-hexose-6-phosphate dehydrogenase-11beta-hydroxyster...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-5
Journal Detail:
Title:  Plant science : an international journal of experimental plant biology     Volume:  203-204C     ISSN:  1873-2259     ISO Abbreviation:  Plant Sci.     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-2-18     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9882015     Medline TA:  Plant Sci     Country:  -    
Other Details:
Languages:  ENG     Pagination:  41-54     Citation Subset:  -    
Copyright Information:
Copyright © 2013 Elsevier Ireland Ltd. All rights reserved.
Affiliation:
Institut de Biologie Moléculaire des Plantes du Centre National de la Recherche Scientifique, IBMP-CNRS-UPR2357, Université de Strasbourg, 28 rue Goethe, F-67083 Strasbourg Cedex, France. Electronic address: Andrea.Hemmerlin@ibmp-cnrs.unistra.fr.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

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


Previous Document:  A rice stress-responsive NAC gene enhances tolerance of transgenic wheat to drought and salt stresse...
Next Document:  Nutrient supply has greater influence than sink strength on photosynthetic adaptation to CO(2) eleva...