title: Alr2954 of Anabaena sp. PCC 7120 with ADP-ribose pyrophosphatase activity bestows abiotic stress tolerance in Escherichia coli.
abstract: In silico derived properties on experimental validation revealed that hypothetical protein Alr2954 of Anabaena sp. PCC7120 is ADP-ribose pyrophosphatase, which belongs to nudix hydrolase superfamily. Presence of ADP-ribose binding site was attested by ADP-ribose pyrophosphatase activity (Km44.71 ± 8.043 mM, Vmax7.128 ± 0.417 μmol min-1mg protein-1, and Kcat/Km9.438 × 104μM-1 min-1). Besides ADP-ribose, the enzyme efficiently hydrolyzed various nucleoside phosphatases such as 8-oxo-dGDP, 8-oxo-dADP, 8-oxo-dGTP, 8-oxo-dATP, GDP-mannose, ADP-glucose, and NADH. qRT-PCR analysis of alr2954 showed significant expression under different abiotic stresses reconfirming its role in stress tolerance. Thus, Alr2954 qualifies to be a member of nudix hydrolase superfamily, which serves as ADP-ribose pyrophosphatase and assists in multiple abiotic stress tolerance.
authors: Molecular Biology Section, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi, 221005, India.
authors: Prashant Kumar
authors: PK
authors: Singh
authors: Department of Chemical Engineering, Indian Institute of Technology, Banaras Hindu University, Vranasi, 221005, India.
authors: Alok Kumar
authors: AK
authors: Shrivastava
authors: Molecular Biology Section, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi, 221005, India.
authors: Shilpi
authors: S
authors: Singh
authors: Molecular Biology Section, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi, 221005, India.
authors: Ruchi
authors: R
authors: Rai
authors: Molecular Biology Section, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi, 221005, India.
authors: Antra
authors: A
authors: Chatterjee
authors: Molecular Biology Section, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi, 221005, India. lcrbhu15@gmail.com.
authors: L C
authors: LC
authors: Rai
mesh_terms: D000246:Adenosine Diphosphate Ribose / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence / Q000235:genetics; D017033:Anabaena / Q000201:enzymology*; D001665:Binding Sites; D003001:Cloning, Molecular; D003198:Computer Simulation; D003838:Deoxyadenine Nucleotides / Q000378:metabolism; D003848:Deoxyguanine Nucleotides / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D006868:Hydrolysis; D062105:Molecular Docking Simulation; D011755:Pyrophosphatases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D013312:Stress, Physiological / Q000235:genetics*; D013379:Substrate Specificity
chemical_list: C089930:8-oxodeoxyadenosine triphosphate; D003838:Deoxyadenine Nucleotides; D003848:Deoxyguanine Nucleotides; C078206:8-oxodeoxyguanosine triphosphate; D000246:Adenosine Diphosphate Ribose; D011755:Pyrophosphatases; C019620:ADPribose pyrophosphatase
keywords: ADP-ribose pyrophosphatase; Anabaena sp. PCC 7120; Cloning and expression; Escherichia coli; Homology modeling; Hypothetical protein; Molecular docking