Flap Endonuclease Activity of Gene 6 Exonuclease of Bacteriophage T7
نویسندگان
چکیده
منابع مشابه
Flap endonuclease of bacteriophage T7
Gene 6 protein of bacteriophage T7 has 5'-3'-exonuclease activity specific for duplex DNA. We have found that gene 6 protein also has flap endonuclease activity. The flap endonuclease activity is considerably weaker than the exonuclease activity. Unlike the human homolog of gene 6 protein, the flap endonuclease activity of gene 6 protein is dependent on the length of the 5'-flap. This dependenc...
متن کاملT7 exonuclease (gene 6) is necessary for molecular recombination of bacteriophage T7.
The role of T7-induced exonuclease (gene 6) in molecular recombination was studied by examining the fate of parental DNA during parental-to-progeny recombination. The method used was to compare infections with T7(+), T7am-6-233 (am gene 6), or T7ts6-136 (ts gene 6) under permissive and nonpermissive conditions. CsCl density gradient analysis of replicative DNA indicated that T7 exonuclease is n...
متن کاملT7 gene 6 exonuclease has an RNase H activity.
T7 gene 6 exonuclease has been shown to have an RNase H activity as well as a double-strand specific DNase activity by the following experiments: The RNase H activity coelutes with the DNase activity from DEAE-cellulose, phosphocellulose, hydroxyapatite, and Sephadex G-200 columns. Gene 6 exonuclease specified by a T7 strain with a temperature sensitive mutation in gene 6 has an extremely heat-...
متن کاملSelective inactivation of the exonuclease activity of bacteriophage T7 DNA polymerase by in vitro mutagenesis.
The 3' to 5' exonuclease activity of bacteriophage T7 DNA polymerase (gene 5 protein) can be inactivated selectively by reactive oxygen species. Differences in the enzymatic properties between the two forms are exploited to show by a chemical screen that modification of a histidine residue reduces selectively the exonuclease activity. In vitro mutagenesis of the histidine at residue 123, and of...
متن کاملRescue of bacteriophage T7 DNA polymerase of low processivity by suppressor mutations affecting gene 3 endonuclease.
The DNA polymerase encoded by gene 5 (gp5) of bacteriophage T7 has low processivity, dissociating after the incorporation of a few nucleotides. Upon binding to its processivity factor, Escherichia coli thioredoxin (Trx), the processivity is increased to approximately 800 nucleotides per binding event. Several interactions between gp5/Trx and DNA are required for processive DNA synthesis. A basi...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2014
ISSN: 0021-9258
DOI: 10.1074/jbc.m113.538611