Mutational analysis of domain II beta of bacteriophage Mu transposase: domains II alpha and II beta belong to different catalytic complementation groups

J Mol Biol. 1998 Jan 16;275(2):221-32. doi: 10.1006/jmbi.1997.1466.

Abstract

This study examines the contribution of domain II beta of bacteriophage Mu transposase (A protein), a subdomain of the central catalytic domain II, to the transposition reaction. The properties of several point mutations implicate a role for this domain in facilitating metal-assisted assembly of the synaptic complex, as well as in intramolecular DNA strand transfer. Point mutations as well as deletions in domain II beta can be complemented by those in domain II alpha but not those in domain III alpha. Thus, residues within subdomains II alpha and II beta belong to different catalytic complementation groups.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacteriophage mu / enzymology*
  • Binding Sites
  • Catalysis
  • Genetic Complementation Test
  • Kinetics
  • Macromolecular Substances
  • Mutagenesis, Site-Directed
  • Point Mutation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Deletion
  • Transposases / chemistry*
  • Transposases / metabolism*
  • Zinc / pharmacology

Substances

  • Macromolecular Substances
  • Recombinant Proteins
  • Transposases
  • Zinc