Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/36411
Title: The SUD1 Gene Encodes a Putative E3 Ubiquitin Ligase and Is a Positive Regulator of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Activity in Arabidopsis
Author: Doblas, Verónica G.
Amorim-Silva, Vítor
Posé, David
Rosado, Abel
Esteban, Alicia
Arró i Plans, Montserrat
Azevedo, Herlander
Bombarely, Aureliano
Borsani, Omar
Valpuesta, Victoriano
Ferrer i Prats, Albert
Tavares, Rui M.
Botella, Miguel A.
Keywords: Enzims
Àrabis
Proteïnes vegetals
Sistemes de control biològic
Àcid mevalònic
Enzymes
Arabis
Plant proteins
Biological control systems
Mevalonic acid
Issue Date: 12-Feb-2013
Publisher: American Society of Plant Physiologists
Abstract: The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) enzyme catalyzes the major rate-limiting step of the mevalonic acid (MVA) pathway from which sterols and other isoprenoids are synthesized. In contrast with our extensive knowledge of the regulation of HMGR in yeast and animals, little is known about this process in plants. To identify regulatory components of the MVA pathway in plants, we performed a genetic screen for second-site suppressor mutations of the Arabidopsis thaliana highly drought-sensitive drought hypersensitive2 (dry2) mutant that shows decreased squalene epoxidase activity. We show that mutations in SUPPRESSOR OF DRY2 DEFECTS1 (SUD1) gene recover most developmental defects in dry2 through changes in HMGR activity. SUD1 encodes a putative E3 ubiquitin ligase that shows sequence and structural similarity to yeast Degradation of a factor (Doa10) and human TEB4, components of the endoplasmic reticulum-associated degradation C (ERAD-C) pathway. While in yeast and animals, the alternative ERAD-L/ERAD-M pathway regulates HMGR activity by controlling protein stability, SUD1 regulates HMGR activity without apparent changes in protein content. These results highlight similarities, as well as important mechanistic differences, among the components involved in HMGR regulation in plants, yeast, and animals.
Note: Reproducció del document publicat a: http://dx.doi.org/10.1105/tpc.112.108696
It is part of: Plant Cell, 2013, vol. 25, num. 2, p. 728-743
Related resource: http://dx.doi.org/10.1105/tpc.112.108696
URI: http://hdl.handle.net/2445/36411
ISSN: 1040-4651
Appears in Collections:Articles publicats en revistes (Bioquímica i Biomedicina Molecular)

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