T4 endonuclease V exists in solution as a monomer and binds to target sites as a monomer

Katherine Atkins Latham, Surendran Rajendran, J. Russ Carmical, James C. Lee, R. Stephen Lloyd

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Endonuclease V, a N-glycosylase/lyase from T4 bacteriophage that initiates the repair of cyclobutane pyrimidine dimers in DNA, has been reported to form a monomer-dimer equilibrium in solution [Nickell and Lloyd (1991) Biochemistry 30, 8638], although the enzyme has only been crystallized in the absence of substrate as a monomer [Morikawa et al. (1992) Science 256, 523]. In this study, analytical gel filtration and sedimentation equilibrium techniques were used to rigorously characterize the association state of the enzyme in solution. In contrast to the previous report, at 100 mM KCl endonuclease V was found to exist predominantly as a monomer in solution by both of these techniques; no evidence for dimerization was seen. To characterize the oligomeric state of the enzyme at its target sites on DNA, the enzyme was bound to oligonucleotides containing a single site-specific pyrimidine dimer or tetrahydrofuran residue. These complexes were analyzed by nondenaturing gel electrophoresis at various acrylamide concentrations in order to determine the molecular weights of the enzyme-DNA complexes. The results from these experiments demonstrate that endonuclease V binds to cyclobutane pyrimidine dimer and tetrahydrofuran site containing DNA as a monomer.

Original languageEnglish (US)
Pages (from-to)324-334
Number of pages11
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Issue number2
StatePublished - Feb 8 1996
Externally publishedYes


  • Cyclobutane pyrimidine dimer
  • Endonuclease V
  • N-glycosylase
  • Protein-DNA interaction
  • Tetrahydrofuran

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology
  • Biophysics
  • Biochemistry


Dive into the research topics of 'T4 endonuclease V exists in solution as a monomer and binds to target sites as a monomer'. Together they form a unique fingerprint.

Cite this