Fig. 1: Biochemical characterization of Mtb-RNase J. | Nature Communications

Fig. 1: Biochemical characterization of Mtb-RNase J.

From: Structural insights into RNase J that plays an essential role in Mycobacterium tuberculosis RNA metabolism

Fig. 1

a Gel filtration profile of full-length Mtb-RNase J on a Superdex200 16/300 column. b SDS-PAGE result of the corresponding fractions in (a). c The β-lactamase activity of Mtb-RNase J with the substrate nitrocefin. d The ribonuclease activity of Mtb-RNase J with 5′-FAM labeled 20-nt poly(U) RNA as the substrate. e, f. Different divalent ions affected the ribonuclease activity of Mtb-RNase J. The concentrations of divalent metal ions and EDTA were 5 mM and 10 mM, respectively. 5′-FAM labeled 20-nt poly(U) RNA was used as the substrate at a concentration of 5 µM. CON: without additional ions; EDTA + Mn2+: chelated with EDTA, then supplemented with Mn2+; EDTA + Zn2+: chelated with EDTA, then supplemented with Zn2+. g Effect of Mn2+ to Mtb-RNase J ribonuclease activity with 20-nt poly(U) RNA as the substrate. h The ribonuclease activity of Mtb-RNase with 20-nt poly(U) RNA as substrate in the presence of 5 mM Mn2+.

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