Expression of genes encoding acetyl-CoA carboxylase, biotin synthase, and acetyl-CoA generating enzymes in Arabidopsis thaliana

1997 ◽  
Author(s):  
Jinshan Ke
PLoS ONE ◽  
2015 ◽  
Vol 10 (3) ◽  
pp. e0119835 ◽  
Author(s):  
Vera S. Bogdanova ◽  
Olga O. Zaytseva ◽  
Anatoliy V. Mglinets ◽  
Natalia V. Shatskaya ◽  
Oleg E. Kosterin ◽  
...  

2011 ◽  
Vol 52 (5) ◽  
pp. 894-908 ◽  
Author(s):  
Hugues Renault ◽  
Abdelhak El Amrani ◽  
Ravishankar Palanivelu ◽  
Emily P. Updegraff ◽  
Agnès Yu ◽  
...  

PLoS ONE ◽  
2014 ◽  
Vol 9 (12) ◽  
pp. e114712 ◽  
Author(s):  
Hongle Xu ◽  
Wenpan Zhang ◽  
Teng Zhang ◽  
Jun Li ◽  
Xian Wu ◽  
...  

2018 ◽  
Vol 29 (9) ◽  
pp. 2326-2336 ◽  
Author(s):  
Mardiana Lee ◽  
Marina Katerelos ◽  
Kurt Gleich ◽  
Sandra Galic ◽  
Bruce E. Kemp ◽  
...  

BackgroundExpression of genes regulating fatty acid metabolism is reduced in tubular epithelial cells from kidneys with tubulointerstitial fibrosis (TIF), thus decreasing the energy produced by fatty acid oxidation (FAO). Acetyl-CoA carboxylase (ACC), a target for the energy-sensing AMP-activating protein kinase (AMPK), is the major controller of the rate of FAO within cells. Metformin has a well described antifibrotic effect, and increases phosphorylation of ACC by AMPK, thereby increasing FAO.MethodsWe evaluated phosphorylation of ACC in cell and mouse nephropathy models, as well as the effects of metformin administration in mice with and without mutations that reduce ACC phosphorylation.ResultsReduced phosphorylation of ACC on the AMPK site Ser79 occurred in both tubular epithelial cells treated with folate to mimic cellular injury and in wild-type (WT) mice after induction of the folic acid nephropathy model. When this effect was exaggerated in mice with knock-in (KI) Ser to Ala mutations of the phosphorylation sites in ACC, lipid accumulation and fibrosis increased significantly compared with WT. The effect of ACC phosphorylation on fibrosis was confirmed in the unilateral ureteric obstruction model, which showed significantly increased lipid accumulation and fibrosis in the KI mice. Metformin use was associated with significantly reduced fibrosis and lipid accumulation in WT mice. In contrast, in the KI mice, the drug was associated with worsened fibrosis.ConclusionsThese data indicate that reduced phosphorylation of ACC after renal injury contributes to the development of TIF, and that phosphorylation of ACC is required for metformin’s antifibrotic action in the kidney.


2009 ◽  
Vol 25 (3) ◽  
pp. 381-395 ◽  
Author(s):  
Hou Yang Kang ◽  
Xing Fan ◽  
Hai Qin Zhang ◽  
Li Na Sha ◽  
Gen Lou Sun ◽  
...  

Botany ◽  
2016 ◽  
Vol 94 (8) ◽  
pp. 615-634 ◽  
Author(s):  
Bianyun Yu ◽  
Margaret Y. Gruber ◽  
Shu Wei ◽  
Rong Zhou ◽  
Dwayne Hegedus ◽  
...  

Despite numerous studies on ABI4, its role in plant secondary metabolism has not been fully investigated. Here, we used metabolite profiling together with transcriptome analysis to demonstrate that ABI4 transcript levels regulate a host of secondary metabolite pathways and growth modalities in ABI4 over-expression (ABI4_OE) lines of Arabidopsis thaliana. This strategy provided a unique and comprehensive overview of the regulation of metabolic shifts in response to ABI4 transcription. We show that enhancement of ABI4 transcript levels changed seed proanthocyanidin (PA), flavonoid, and carotenoid levels in ABI4_OE seeds and 30-day-old shoots, as well as the expression of genes encoding enzymes involved in the production of these and other secondary metabolites in ABI4_OE shoots. In seeds, PA accumulated in very large uneven patches, which was dramatically different from the even distribution of PA in wild-type seeds. Shoots of ABI4_OE lines also exhibited altered expression of a range of genes involved in several aspects of plant development, including hormone and cell-wall synthesis. Alteration of such disparate secondary metabolite pathways, along with hormone and developmental pathways, suggests that ABI4 is a master regulator integrating these compounds with plant development.


2021 ◽  
Vol 23 (1) ◽  
pp. 409
Author(s):  
Anna Janik ◽  
Urszula Perlińska-Lenart ◽  
Katarzyna Gawarecka ◽  
Justyna Augustyniak ◽  
Ewelina Bratek-Gerej ◽  
...  

Protein glycosylation requires dolichyl phosphate as a carbohydrate carrier. Dolichols are α-saturated polyprenols, and their saturation in S. cerevisiae is catalyzed by polyprenyl reductase Dfg10 together with some other unknown enzymes. The aim of this study was to identify such enzymes in Candida. The Dfg10 polyprenyl reductase from S. cerevisiae comprises a C-terminal 3-oxo-5-alpha-steroid 4-dehydrogenase domain. Alignment analysis revealed such a domain in two ORFs (orf19.209 and orf19.3293) from C. albicans, which were similar, respectively, to Dfg10 polyprenyl reductase and Tsc13 enoyl-transferase from S. cerevisiae. Deletion of orf19.209 in Candida impaired saturation of polyprenols. The Tsc13 homologue turned out not to be capable of saturating polyprenols, but limiting its expression reduce the cellular level of dolichols and polyprenols. This reduction was not due to a decreased expression of genes encoding cis-prenyltransferases from the dolichol branch but to a lower expression of genes encoding enzymes of the early stages of the mevalonate pathway. Despite the resulting lower consumption of acetyl-CoA, the sole precursor of the mevalonate pathway, it was not redirected towards fatty acid synthesis or elongation. Lowering the expression of TSC13 decreased the expression of the ACC1 gene encoding acetyl-CoA carboxylase, the key regulatory enzyme of fatty acid synthesis and elongation.


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