Native gel electrophoresis reveals an interaction between SycO and YscM1. Recombinant proteins as indicated were loaded on Tris-buffered native gels. The gels were Coomassie-stained (A) or alternatively electro-blotted and incubated with antisera raised against SycO (B), and YscM1 (C), respectively. The amount of SycO (20 μg) was approximately equimolar to that of YscM1 (15 μg) and YscM2 (15 μg). SycO/YscM1 complex is indicated by arrowheads. YscM2 does not enter the native gel (pH 8) due to its high isoelectric point (pI 9.79).