Bacteriophage XP-12-induced exonuclease which preferentially hydrolyzes nicked DNA.
AUTOR(ES)
Farber, M B
RESUMO
An exonuclease has been partially purified from XP-12-infected Xanthomonas oryzae which is not found in uninfected X. oryzae. Although both the phage-induced exonuclease and the major host exonucleolytic DNase released 5'-mononucleotides, these enzymes differed in their chromatographic behavior, pH optimum, salt inhibition, and heat sensitivity. These two exonucleases preferred different substrates. Nicked native DNA was the best substrate for the phage-induced enzyme, whereas denatured DNA was the best substrate for the host enzyme. Also, the host enzyme had a significant preference for denatured or nicked, normal cytosine-containing DNA (e.g., X. oryzae or T7 DNA) over similarly denatured or nicked 5-methylcytosine-rich DNA (namely, XP-12DNA), whereas the phage-induced enzyme hydrolyzed both types of DNA equally well.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=288598Documentos Relacionados
- 5-methyl-dCTP deaminase induced by bacteriophage XP-12.
- Exonuclease associated with bacteriophage T5-Induced DNA polymerase.
- Role of the T5 gene D15 nuclease in the generation of nicked bacteriophage T5 DNA.
- A covalent complex between retroviral integrase and nicked substrate DNA.
- The use of phosphorothioate-modified DNA in restriction enzyme reactions to prepare nicked DNA.