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 m 44.71 ± 8.043 mM, V max 7.128 ± 0.417 μmol min−1 mg protein−1, and K cat/K m 9.438 × 104 μM−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.
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Acknowledgments
L.C. Rai is thankful to the CSIR, ICAR, DST for J.C. Bose National Fellowship and DAE for Raja Ramanna Fellowship. Alok Kumar Shrivastava is thankful to SERB New Delhi for Young Scientist award. Antra Chatterjee to the UGC, New Delhi, for JRF. Shilpi Singh and Ruchi Rai to DST for WOSA award. We thank the Head Botany and the Programe coordinator Centre of Advanced Study in Botany for facilities.
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Singh, P.K., Shrivastava, A.K., Singh, S. et al. Alr2954 of Anabaena sp. PCC 7120 with ADP-ribose pyrophosphatase activity bestows abiotic stress tolerance in Escherichia coli . Funct Integr Genomics 17, 39–52 (2017). https://doi.org/10.1007/s10142-016-0531-y
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DOI: https://doi.org/10.1007/s10142-016-0531-y