AAA+ superfamily ATPases: common structure–diverse function

By T. Ogura, A. Wilkinson. Genes to Cells, 2001

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Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains. (2003, background): “2000); RuvB, which promotes DNA branch migration at Holliday junctions during genetic recombination; and the clamp loader g complex, which opens the b sliding clamp ring and loads it onto DNA to mediate processive movement of DNA polymerase (Neuwald et al. 1999; Vale 2000; Jeruzalmi et al. 2001a; Je”
Metabolism of Rhizobium Bacteroids (2003, background): “AAA-like genes are widespread, although their mode of action is still unclear (Confalonieri and Duguet, 1995; Ogura and Wilkinson, 2001).”
Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective (2012, background): “menclature for dynein has been standardized [545]. Its large head consists of 6 domains arranged in the form a ring that is a typical characteristics of the members of the AAA+ superfamily of ATPases [546, 547, 548, 549, 550, 551, 552, 553]. However, compared to the other members of the AAA+ superfa”
AAA+ proteins: have engine, will work (2005, background): “We hope that this review serves as both an introduction to, and an update on, this important family of ATPases (for other reviews of AAA+ proteins, see Ref”