Purification and properties of the ribonucleic acid-dependent ribonucleic acid polymerase from Halobacterium cutirubrum
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منابع مشابه
Purification and properties of the ribonucleic acid-dependent ribonucleic acid polymerase from Halobacterium cutirubrum.
1. The RNA-dependent RNA polymerase from Halobacterium cutirubrum was purified to electrophoretic homogeneity. 2. It requires a single-stranded molecule of RNA or polyribonucleotide as template. 3. Nearest-neighbour analyses of the products formed on random poly(A,U) or alternating poly(A-U) templates and base analysis of the product of synthesis directed by wheat-germ RNA prove that the templa...
متن کاملHALOBACTERIUM CUTIRUBRUM DEOXYRIBONUCLEIC ACID-DEPENDENT RIBONUCLEIC ACID POLYMERASE By B. GREGORY LOUIS AND P. S. FITT
1. DNA-dependent RNA polymerase was purified 150-fold from crude extracts of the extreme halophile Halobacterium cutirubrum. 2. The enzyme requires the presence of native DNA and all four nucleoside triphosphates to incorporate '4C-labelled nucleoside triphosphate into an acid-insoluble ribonuclease-sensitive product. 3. It has an absolute requirement for both Mn2+ and Mg2+. 4. The polymerase r...
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It has become evident that several enzymatic reactions exist which lead to the incorporation of the mononucleotide moiety of the ribonucleoside triphosphates into ribonucleic acid (1). The first of these enzymes to be characterized catalyzes the addition of cytosine 5’-phosphate and adenosine 5’-phosphate to the nucleoside terminal end of soluble ribonucleic acid (2,3). The product of this reac...
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NaClO(4) was employed in a technique for the rapid extraction of reovirus ribonucleic acid (RNA). The extracted RNA, which was purified in a Cs(2)SO(4) equilibrium density gradient, had a buoyant density of 1.61 g/cm(3) and a sedimentation coefficient of 15S in a 7 to 20% sucrose gradient. It was 90% resistant to ribonuclease in a solution of high ionic strength (0.1 m NaCl). The sensitivity of...
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Deoxyribonucleic acid (DNA)-dependent ribonucleic acid (RNA) polymerase (EC 2.7.7.6) from Acinetobacter calcoaceticus was purified to apparent homogeneity and its properties were compared with those of the Escherichia coli B enzyme. The molecular weights of the two native active enzymes as well as their alpha and beta subunits appeared to be similar. No subunit corresponding to that of sigma fr...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1972
ISSN: 0306-3283
DOI: 10.1042/bj1280755