Cloning, Expression, and Biochemical Characterization of Hexahistidine-tagged Terminase Proteins*
The results suggest that the hexa-His-tagged holoenzyme possesses a mild DNA-binding defect that is masked, at least in part, by integration host factor.
Mutations That Extend the Specificity of the Endonuclease Activity of λ Terminase
The twofold rotational symmetry of cosN suggests that symmetrically disposed gpA subunits are responsible for nicking cosNL and cosNR, which is thought to interact with cosB, the terminase binding site of gpNu1 and gpA.
Identification, expression, and purification of a unique stable domain from human HSPC144 protein.
Mutations that extend the specificity of the endonuclease activity of lambda terminase.
Results suggest that A-E515G plays an indirect role in extending the specificity of the endonuclease activity of lambda terminase, and in vitro cos cleavage experiments on cosN G2C C11G DNA showed that the rate of cleavage for A- E515G terminase is three- to fourfold higher than for wild-type terminase.