Scheme model summarizing the ATP-dependent and phosphorylation-dependent regulation of AfsR.

Abstract

Unmodified full-length AfsR is autoinhibited by its C-terminal domains. AfsR is activated by ATP binding and significantly stimulates the production of transcripts. The phosphorylation of AfsR results in increased ATPase activity, potentially counteracting the effects of ATP binding. Phosphorylated AfsR forms more oligomers and shows slightly higher transcriptional activation compared to the unmodified form. (TIF)</p