Behavior of Tn3 resolvase in solution and its interaction with res

11Citations
Citations of this article
26Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

The solution properties of Tn3 resolvase (Tn3R) were studied by sedimentation equilibrium, sedimentation velocity analytical ultracentrifugation, and small-angle neutron scattering. Tn3R was found to be in a monomer-dimer self-association equilibrium, with a dissociation constant of KD1-2 = 50μM. Sedimentation velocity and small-angle neutron scattering data are consistent with a solution structure of dimeric Tn3R similar to that of γδ resolvase in a co-crystal structure, but with the DNA-binding domains in a more extended conformation. The solution conformations of sites I, II, and III were studied with small angle x-ray scattering and modeled using rigid-body and ab initio techniques. The structures of these sites do not show any distortion, at low resolution, from B-DNA. The equilibrium binding properties of Tn3R to the individual binding sites in res were investigated by employing fluorescence anisotropy measurements. It was found that site II and site III have the highest affinity for Tn3R, followed by site I. Finally, the affinity of Tn3R for nonspecific DNA was assayed by competition experiments. © 2005 by the Biophysical Society.

Cite

CITATION STYLE

APA

Nöllmann, M., Byron, O., & Stark, W. M. (2005). Behavior of Tn3 resolvase in solution and its interaction with res. Biophysical Journal, 89(3), 1920–1931. https://doi.org/10.1529/biophysj.104.058164

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free