<i>In vitro</i> methylation of PRPL11 by PrmA-like.

<p>(a,b) Kinetic analysis of PRPL11 methylation by PrmA-like. Purified recombinant PRPL11 (2.5 µg) and PrmA-like (0.25 µg) were incubated at 30°C with 20 µM [methyl-³H]-AdoMet. Radioactivity incorporated into proteins was counted by liquid scintillation (a) or analyzed by phosphorimaging (b). A time-course analysis representative of three repeats is shown. The activity (2.0±0.2 nmol methyl incorporated. min⁻¹.mg⁻¹ protein) was strictly dependent on the presence of PrmA-like. (c) Screening of five chloroplastic PKMTs for their ability to methylate PRPL11. Purified recombinant PRPL11 (10 µg) and PKMTs (1 µg) were incubated at 30°C for 15 min with 20 µM [methyl-³H]-AdoMet and radioactivity incorporated into proteins was counted by liquid scintillation. Enzyme nomenclature is as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0095512#pone-0095512-t001" target="_blank">Table 1</a>. Values are mean ± SD of three determinations.