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. 2020 Nov 12;11:610179. doi: 10.3389/fmicb.2020.610179

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Copyright © 2020 Völkner, Jost and Pfeifer.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Split-GFP interaction studies with GvpA/GvpX. Only the highest relative fluorescence determined for each combination is given. Two biological and three technical replicates were performed in each case. (A) Interaction study of GvpA with the eight accessory proteins GvpF through GvpM. (B) Interaction of five different GvpA fragments with GvpF. (C) Sequence of the five GvpA fragments in relation to the aa sequence of GvpA shown on top. Numbers above the sequence depict the aa positions in GvpA. The helices α1 and α2 and the β-sheets β1 and β2 are in bold and marked on the bottom and also shaded in gray.