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. 2020 Jun 13;21(12):4212. doi: 10.3390/ijms21124212

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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The RpoE sigma factor is one of the substrates of FkpB. (A) Co-purification profile of the wild-type FkpB protein and its derivatives N126A, P128A, E86A and with N126A H127 double mutation after the induction in a Δ6ppi derivative with 100 μM IPTG. Proteins were resolved on a 12.5% SDS-PAGE and co-eluting proteins are indicated and their identity shown. (B) Picture of dried 2-D gels of purified FkpB and co-eluting RpoE. The identity of the spot corresponding to RpoE was obtained from MALDI-TOF and is indicated. (C) 2-D gel of purified FkpB variant N126A H127. (D) The PPIase activity in the chymotrypsin-coupled assay with 0.5 μM purified of above mentioned FkpB variants in comparison to the wild type is plotted. (E) Position of various FkpB residues, which were mutated, is indicated in the structure of FkpB (PDB 4DT4).