Alr2954 of Anabaena sp. PCC 7120 with ADP-ribose pyrophosphatase activity bestows abiotic stress tolerance in Escherichia coli.

Prashant Kumar Singh, Alok Kumar Shrivastava, Shilpi Singh, Ruchi Rai, Antra Chatterjee, L C Rai

Journal: Functional & integrative genomics 2017;17(1):39-52

PMID: 27778111

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 (K 44.71 ± 8.043 mM, V 7.128 ± 0.417 μmol min mg protein, and K /K 9.438 × 10 μM1 min). 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.

Address: Molecular Biology Section, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi, 221005, India.; Department of Chemical Engineering, Indian Institute of Technology, Banaras Hindu University, Vranasi, 221005, India.; Molecular Biology Section, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi, 221005, India. [email protected].

DOI: 10.1007/s10142-016-0531-y