Reverse gyrase domains

Reverse gyrases have been purified from a number of organisms from both the Bacteria and Archaea Domains. More recently, recombinant versions have been... 

Fig. 4. Primary structure of reverse gyrases. (A) Schematic representation of reverse gyrase sequence with its two domains comparison of the N-terminal domain with various helicases. elF4A is an eukaryotic initiation factor for translation [J. P. Nielson and H. Trachsel, EMBOJ. 7,2097 (1988)]. PriA is a component of the primosome in bacteria (P Nurse, R. J. DiGate, K. H. Zavitz, and K. J. Marians, Proc. Natl. Acad. Sci. U.S.A. 87,4615 (1990)). Sgsl is a helicase interacting with topoisomerases II and III in yeast [S. Gangloff, J. P McDonald, C. Bendixen, L. Arthur, and R. Rothstein, Mol. Cell Biol. 14, 8391 (1994)]. (B). Amino acid sequences of the helicase motifs in reverse gyrases. x indicates a hydrophobic residue. The sequences shown are a consensus where at least four positions out of six are conserved in reverse gyrases.

Fig. 5. Models for positive supercoiling by reverse gyrases. (A) Dynamic modei based on the tracking of DNA by the helicase-like domain. (B) Static model domains I and II refer to as DNA domains in a circular molecule.

---