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. 2018 Apr 18;9:504. doi: 10.3389/fpls.2018.00504

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Copyright © 2018 Lopes, Rodrigues, Silva, Braga and Silva-Filho.

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 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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FIP is a transmembrane protein containing a zinc-finger domain and is localized in the thylakoid membrane. (A) Amino acid sequence of FIP protein. The transit peptide, transmembrane domain (TMD), and zinc-finger domain are marked. (B) Theoretical model for FIP topology predicted by PROTTER online software. FIP is anchored in thylakoids by TMD and has an amino proximal luminal domain and a carboxyl proximal stromal domain. (C) glutathione S-transferase (GST) pull-down assay of the FtsH5 and FIP interaction. GST and GST-FIP fusion proteins were expressed in Escherichia coli and purified with a GST column. GST and GST-FIP were incubated with nickel resin-purified recombinant FtsH5 fusion protein, pulled down with GST-beads, and detected using an anti-FtsH5 antibody by Western blot analysis.