Open AccessDinucleotides as Products of an Exonucleolytic Activity Associated with the Micrococcus luteus DNA Polymerase
Author(s) -
Steven J. Harwood,
Paul F. Schendel,
Lois K. Miller,
Robert D. Wells
Publication year - 1970
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.66.3.595
Subject(s) - micrococcus luteus , exonuclease , dna polymerase , nuclease , biochemistry , polymerase , dna , enzyme , dna polymerase i , endonuclease , microbiology and biotechnology , biology , dna clamp , micrococcus , chemistry , polymerase chain reaction , bacteria , reverse transcriptase , escherichia coli , genetics , gene
The partially purified DNA polymerase fromMicrococcus luteus contains a low level of exonucleolytic activity. The enzyme preparation (1200-fold purified) contains approximately 100 times more polymerase than exonuclease activity. Both single- and double-stranded DNA are degraded at the same rate. The predominant products are dinucleoside diphosphates (d-pXpY); mononucleotides and a trace of trinucleotides are also produced. Each of these products is formed at a constant rate throughout the course of the reaction. The nuclease degrades a DNA chain from the 5′-end. The enzyme preparation contains no detectable endonuclease activity.