Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancer

Abstract

BACTERIOPHAGE Mu is the largest and most efficient transposable element known1. The Mu transposase (A protein) of relative molecular mass 75,000 is a central component of the transposition machinery2. We report here that the N-terminal region of Mu transposase contains two distinct DNA-binding domains, one which binds the two Mu DNA ends, and another which binds an internal operator region. This internal operator is required for the transposase-mediated synapsis and nicking of Mu ends in vitro, and stimulates transposition more than 100-fold in vivo. The orientation of the operator with respect to the ends is critical to its function, whereas its distance from the ends seems to be relatively unimportant. We propose that the operator enhances transposition by transiently interacting with the transposase and Mu DNA end(s) to form a complex in which synapsis of the ends occurs.