The role of acetyl-coenzyme a synthetase in Arabidopsis.
نویسندگان
چکیده
The acs1 knockout mutant that has a disruption in the plastidic acetyl-coenzyme A (CoA) synthetase (ACS; At5g36880) gene was used to explore the role of this protein and plastidic acetate metabolism in Arabidopsis (Arabidopsis thaliana). Disruption of the ACS gene decreased ACS activity by 90% and largely blocked the incorporation of exogenous (14)C-acetate and (14)C-ethanol into fatty acids. Whereas the disruption had no significant effect on the synthesis of bulk seed triacylglycerols, the acs1 plants were smaller and flowered later. This suggests that the pyruvate dehydrogenase bypass provided by the aerobic fermentation pathway that converts pyruvate to acetate and probably on to fatty acids is important to the plants during normal growth. The role of ACS in destroying fermentative intermediates is supported by the increased sensitivity of the acs1 mutant to exogenous acetate, ethanol, and acetaldehyde compared to wild-type plants. Whereas these observations suggest that flux through the aerobic fermentation pathway is important, the reason for this flux is unclear. Interestingly, acetate is able to support high rates of plant growth on medium and this growth is blocked in the acs1 mutant.
منابع مشابه
The role of pyruvate dehydrogenase and acetyl-coenzyme A synthetase in fatty acid synthesis in developing Arabidopsis seeds.
Acetyl-coenzyme A (acetyl-CoA) formed within the plastid is the precursor for the biosynthesis of fatty acids and, through them, a range of important biomolecules. The source of acetyl-CoA in the plastid is not known, but two enzymes are thought to be involved: acetyl-CoA synthetase and plastidic pyruvate dehydrogenase. To determine the importance of these two enzymes in synthesizing acetyl-CoA...
متن کاملThe Role of Acetyl-CoA Synthetase in Arabidopsis
The acs1 knockout mutant that has a disruption in the plastidic acetyl-CoA synthetase (ACS, At5g36880) gene was used to explore the role of this protein and plastidic acetate metabolism in Arabidopsis thaliana. Disruption of the ACS gene decreased acetyl-CoA synthetase activity by 90% and largely blocked the incorporation of exogenous C-acetate and C-ethanol into fatty acids. While the disrupti...
متن کاملCharacterization of the Arabidopsis thaliana acetyl-CoA synthetase putative carboxylate binding pocket
Acetyl-CoA synthetase catalyzes the activation of acetate by the acetylation of the thiol group of Coenzyme A, while hydrolyzing ATP to AMP and pyrophosphate. The Arabidopsis thaliana acetyl-CoA synthetase (atACS) was compared to other acyl-CoA synthetases, and was computationally modeled on the available crystal structures of the Saccharomyces cerevisiae ACS1 and Salmonella enterica ACS. This ...
متن کاملSpinach leaf acetyl-coenzyme a synthetase: purification and characterization.
Acetyl-coenzyme A (CoA) synthetase was purified 364-fold from leaves of spinach (Spinacia oleracea L.) using ammonium sulfate fractionation followed by ion exchange, dye-ligand, and gel permeation chromatography. The final specific activity was 2.77 units per milligram protein. The average M(r) value of the native enzyme was about 73,000. The Michaelis constants determined for Mg-ATP, acetate, ...
متن کاملHolocarboxylase Synthetase 1 Physically Interacts with Histone H3 in Arabidopsis
Biotin is a water-soluble vitamin required by all organisms, but only synthesized by plants and some bacterial and fungal species. As a cofactor, biotin is responsible for carbon dioxide transfer in all biotin-dependent carboxylases, including acetyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, and pyruvate carboxylase. Adding biotin to carboxylases is catalyzed by the enzyme holocarboxylas...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Plant physiology
دوره 147 4 شماره
صفحات -
تاریخ انتشار 2008