Fig. 3: Probing dimerization and RNA association by targeted mutations of full-length rA3G. | Nature Communications

Fig. 3: Probing dimerization and RNA association by targeted mutations of full-length rA3G.

From: Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G

Fig. 3: Probing dimerization and RNA association by targeted mutations of full-length rA3G.The alternative text for this image may have been generated using AI.

a–c The SDS-PAGE protein gel analysis of the His6-sumo-rA3G WT and various mutants after nickel affinity column purification (a), and 20% denaturing urea polyacrylamide gel analysis of RNAs associated with the proteins without RNase A treatment during purification (b) or with RNase A treatment during purification (c) (see methods for details). d, e Superdex-200 size exclusion chromatography (SEC) analysis of the sumo-rA3G WT and mutant proteins before (d) and after (e) RNase A treatment. The positions corresponding to void volume, dimer, and monomer are indicated with arrows. Source data for all panels are provided in the Source Data file.

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