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O-acetylserine(thiol)lyase and regulates arsenic accumulation in rice
Published in Yong-Guan Zhu, Huaming Guo, Prosun Bhattacharya, Jochen Bundschuh, Arslan Ahmad, Ravi Naidu, Environmental Arsenic in a Changing World, 2019
Complexation of arsenite by thiols is an important mechanism of arsenic (As) detoxification in non-hyperaccumulating plants. Plants could decrease the translocation of As from roots to shoots by increasing the synthesis of a range of thiol-containing compounds in roots (Liu et al., 2010). Cysteine biosynthesis is a central metabolic pathway to incorporate inorganic sulfur into organic molecules. In plants, cysteine is synthesized from O-acetyl-L-serine and sulfide by O-acetylserine(thiol)lyase (OAS-TL). OAS-TL activity is present in the cytosol, plastids and mitochondria (Hell et al., 2002). In the present study, we investigated the As accumulation of rice (Oryza sativa) T-DNA insertion mutants for OsRCS3.
Transcription of genes associated with nickel resistance induced by different doses of nickel nitrate in Quercus rubra
Published in Chemistry and Ecology, 2019
Charnelle L. Djeukam, Paul Michael, Kabwe K. Nkongolo
Another gene of interest is the gene which encodes for serine acetyltransferase (SAT). This enzyme catalyses the acetylation reaction of L-serine to produce O-acetyl-L-serine, a positive regulator of sulfur assimilation and an intermediate in the biosynthesis of the amino acid cysteine. When a plant is exposed to high levels of Ni, this enzyme is overexpressed to counteract the harmful effects of oxidative stress [23]. In the present study, the differential transcription of this gene in leaves of plants treated with 1600 mg/kg of Ni nitrate is due to Ni because potassium nitrate resulted in a downregulation of SAT transcription compared to water. This suggests that the transcription of this gene is affected by high doses of Ni. These results are similar to report on Cd regulation in Arabidopsis thaliana that showed high SAT expression at high Cd concentrations [1]. A comparative analysis of Thlaspi goingense and A. thaliana revealed that T. goesingense (a Ni accumulator) exhibits a higher activity of the SAT enzyme which is partly responsible for the Ni tolerance observed in this species [23,48]. Previous studies have demonstrated high expression of this gene at the root level compared to leaves in Arabidopsis [49]. Our results confirmed this observation because the transcription of SAT was higher in roots compared to leaves in samples treated with 800 mg/kg. Lack of amplification of this gene in root samples treated with 150 mg/kg of potassium nitrate may be the result of the degradation of the synthesised cDNA or the presence of an inhibitor.
Recombinant production of active Streptococcus pneumoniae CysE in E. coli facilitated by codon optimized BL21(DE3)-RIL and detergent
Published in Preparative Biochemistry and Biotechnology, 2019
Deepali Verma, Monika Antil, Vibha Gupta
The cysteine amino acid, containing thiol moiety, is involved in many cellular functions and is also a constituent of several biomolecules.[5]De novo cysteine biosynthesis is a conserved pathway in bacteria.[6,7] This pathway comprises two enzymes namely (i) Serine acetyltransferase (SAT) or CysE which catalyzes the formation of O-acetyl- L-serine (OAS) from L-serine and acetyl-CoA and (ii) Pyridoxal 5' phosphate-dependent O-acetylserine sulfhydrylase (OASS) or CysK, that converts OAS in the presence of sulfide or thiosulfate to L-cysteine (Fig. 1).[8] Fortunately, biosynthesis of cysteine follows a different route in humans and both CysE and CysK are absent in Homo sapiens.[9]cysE gene is listed as essential in the Database of Essential Genes (DEG) [10] for several human pathogens such as E. coli,[10]H. influenza,[11]S. aureus,[12]M. tuberculosis,[7,13,14] and B. subtilis.[6] As CysE appears to be essential for multiple bacterial species, its inhibition in S. pneumoniae may also be disruptive to its growth.