The mechanisms of action of E. coli endonuclease III and T4 UV endonuclease (endonuclease V) at AP sites.
AUTOR(ES)
Kim, J
RESUMO
Treatment of DNA containing AP sites with either T4 UV endonuclease or with E. coli endonuclease III followed by a human class II AP endonuclease releases a putative beta-elimination product. This result suggests that both the T4 endonuclease and E. coli endonuclease III class I AP endonucleases catalyze phosphodiester bond cleavage via a lyase- rather than a hydrolase mechanism. Indeed, we have not detected a class I AP endonuclease which hydrolytically catalyzes phosphodiester bond cleavage. Whereas these enzymes use a lyase-like rather than a hydrolytic mechanism, they nonetheless catalyze phosphodiester bond cleavage. We suggest that the term endonuclease can be properly applied to them.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=334742Documentos Relacionados
- Processive action of T4 endonuclease V on ultraviolet-irradiated DNA.
- Specific action of T4 endonuclease V on damaged DNA in xeroderma pigmentosum cells in vivo.
- A Mutant of E. COLI That Restricts Growth of Bacteriophage T4 at Elevated Temperatures
- Synthesis and characterization of a substrate for T4 endonuclease V containing a phosphorodithioate linkage at the thymine dimer site.
- The interaction of T4 endonuclease V E23Q mutant with thymine dimer- and tetrahydrofuran-containing DNA.