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. 2018 Feb 5;46(7):3753–3763. doi: 10.1093/nar/gky050

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — VgaA_LC activity requires mM-range concentrations of NTP nucleotides (ATP, GTP, CTP or UTP) and is not sustained either by the non-hydrolysable ATP analogue ADPNP, the slow-hydrolysable analogue ATPγS nor the product of ATP hydrolysis, ADP. Puromycin reactivity is progressively rescued by 1 μM VgaA_LC and increasing concentrations ATP (A) or by increasing concentrations VgaA_LC in the presence of constant 1 mM ATP (B). The resistance effect saturates at 0.5 mM ATP and 0.5 μM VgaA_LC, respectively. VgaA_LC-mediated rescue of puromycin reactivity is supported by either ATP, GTP, CTP or UTP nucleotides added at 1 mM, suggesting that VgaA_LC is an NTPase, rather than a strict ATPase (C). Neither ADP, nor the non-hydrolysable ATP analogue ADPNP nor the slow-hydrolysable analogue ATPγS can support VgaA_LC activity, indicating that NTP hydrolysis, not just the NTP binding, are necessary (D).