An interaction between the respiratory enzyme fumarate reductase (Frd, also known as Complex II) and an ATPase has been identified in E. coli by the Houry lab. The research shows that the RavA ATPase, belonging to a poorly characterized but ubiquitous MoxR family of AAA+ ATPases, associates with the Frd respiratory enzyme through an adaptor, which the group named ViaA. This interaction was further shown to modulate the activity of Frd. RavA-ViA were also found to affect another respiratory enzyme, Complex I (also known as NADH:ubiquinone oxidoreductase or nuo). Hence, RavA-ViaA could function as a novel regulatory element involved in cellular respiration of E. coli.
Reference for the paper:
Wong, K. S., Bhandari, V., Janga, S. C., & Houry, W. A. “The MoxR AAA+ ATPase RavA and its Cofactor ViaA Interact with and Modulate the Activity of the Fumarate Reductase Complex during Anaerobiosis in Escherichia coli” Journal of Molecular Biology 429(2), 324–344 (2017).