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. 2016 May 6;101(2):314–332. doi: 10.1111/mmi.13392

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© 2016 The Authors Molecular Microbiology Published by John Wiley & Sons Ltd

This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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Identification of the Aar domains required for homo‐dimerization.

Amino acids involved in homo‐oligomerization of Aar were determined by the BACTH system (depicted in blue, Panel A). pKNTAar derivatives carrying mutations in aar were co‐transformed with pUT18Aar into E. coli BTH101. Bacterial cultures were analyzed for β‐galactosidase activity (Panel B and D). Oligomeric states of Aar with two different tag were analyzed in bacterial preps (Panel C and E). Recombinant Aar‐MBP protein was cleaved with factor Xa, heated under denaturing conditions and analyzed by SDS‐PAGE gels (Panel C). Whole preps of E. coli DH5α transformed with pGBKT7 and pGBKT7Aar were analyzed by Western blot using specific antibodies for Myc tag (Panel E). Data are representative of at least three independent experiments. Statistical significance compared to the negative control was assessed by ANOVA (**, P < 0.001).