Ribonuclease H from chick embryos cleaves precisely at the junction between the RNA and DNA portion of the hybrid helix.
DNA polymerase from Micrococcus luteus and RNA polymerase from E. coli catalyze the synthesis of poly(dA) with poly(dT) template, in the presence of ATP and [alpha-32P]dATP. The reaction is completely dependent on poly(A) primer synthesis. Poly(A) chains are covalently extended by DNA polymerase. Primer poly(A) is linked to the product poly(dA) via a 3':5'-phosphodiester bond, and can be specifically removed by ribonuclease H from chick embryos, leaving a 5'-phosphate end of poly(dA). The length of RNA and DNA products appears to be relatively variable. The size of the DNA is less than 3 000 nucleotides.
D000818:Animals; D002642:Chick Embryo; D004247:DNA / Q000378:metabolism*; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D004722:Endoribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D008837:Micrococcus / Q000201:enzymology; D011061:Poly A / Q000096:biosynthesis* / Q000378:metabolism; D011071:Poly T / Q000378:metabolism; D012313:RNA / Q000378:metabolism*; D016914:Ribonuclease H; D013698:Templates, Genetic
D011061:Poly A; D011071:Poly T; C037095:poly(A)-poly(dA); D012313:RNA; D004247:DNA; D012321:DNA-Directed RNA Polymerases; D004259:DNA-Directed DNA Polymerase; D004722:Endoribonucleases; D016914:Ribonuclease H