Abstract
A DNA polymerase activity isolated from purified wheat embryo mitochondria has been characterized. The enzyme is confined to the matrix of the organelle as shown after treatment with digitonin and sonication. After DEAE-cellulose, phosphocellulose, DNA-cellulose and Sephacryl 200 SF chromatography, only one peak of activity has been found. The mitochondrial DNA polymerase recognizes very efficiently activated DNA as well as poly(dA-dT 12), but very poorly poly(A-dT 12) in the presence of manganese and not at all in the presence of magnesium. The wheat mitochondrial polymerase is completely resistant to N-ethylmaleimide, slightly inhibited by ddTTP and ethidium bromide. The template specificity and the effect of inhibitors on this polymerase are very different to those described for the animal mitochondrial DNA polymerase. We conclude that the plant mitochondrial DNA polymerase is not a DNA polymerase of the γ type.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
