title: Ribonuclease H from chick embryos cleaves precisely at the junction between the RNA and DNA portion of the hybrid helix.
abstract: 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.
mesh_terms: 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
chemical_list: 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