A serine involved in actin-dependent subcellular localization of a stress-induced tobacco BY-2 hydroxymethylglutaryl-CoA reductase isoform

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A hydroxymethylglutaryl-CoA reductase inhibitor synthesized by yeasts.

Screening of different yeast species showed that they are able to synthesize hydroxymethylglutaryl-CoA (HMGCoA) reductase inhibitors. Crude methanol extracts and the purified inhibitors from Pichia labacensis and Candida cariosilignicola were tested for their biological activity on the solubilized microsomal HMGCoA reductase from Chinese hamster ovary cells. Identification of the inhibitors was...

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Regulation of hydroxymethylglutaryl-CoA reductase in rat leukocytes.

Methods were developed for the assay of hydroxymethylglutaryl-CoA reductase (NADPH) activity in microsomes from rat leukocytes. The activity in freshly isolated leukocytes is low compared to rat liver but can be assayed reliably. The patterns of response of leukocyte reductase in the assay to variation in substrate concentration, protein concentration, and time mimic those of rat liver reductas...

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Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system.

Protein phosphatase C was purified 1500-fold from rat liver by a six-step procedure including a fractionation step with 80% ethanol at room temperature and two successive chromatographic separations on DEAESephadex. This preparation restored hydrox~ethyl glutaryl-CoA (HMG-CoA) reductase activity in liver microsomes pretreated with MgATP and also inactivated HMG-CoA reductase kinase. The relativ...

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The subcellular localization of acetyl-CoA carboxylase 2.

Animals, including humans, express two isoforms of acetyl-CoA carboxylase (EC ), ACC1 (M(r) = 265 kDa) and ACC2 (M(r) = 280 kDa). The predicted amino acid sequence of ACC2 contains an additional 136 aa relative to ACC1, 114 of which constitute the unique N-terminal sequence of ACC2. The hydropathic profiles of the two ACC isoforms generally are comparable, except for the unique N-terminal seque...

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Hydroxymethylglutaryl CoA reductase and the modulation of microsomal cholesterol content by the nonspecific lipid transfer protein.

The influence of membrane cholesterol content on 3-hydroxy-3-methylglutaryl CoA reductase (HMG-CoA reductase, EC 1.1.1.34) in rat liver microsomes was investigated. Microsomes were enriched in cholesterol by incubation with egg phosphatidylcholine-cholesterol vesicles and the nonspecific lipid transfer protein from rat liver. By this method, the microsomal cholesterol content was 2.5-fold enhan...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 2007

ISSN: 0014-5793

DOI: 10.1016/j.febslet.2007.10.023