Phosphorolysis of oligoribonucleotides by polynucleotide phosphorylase.
نویسنده
چکیده
This reversible reaction has been demonstrated With enzyme preparations from Azotobacter trinelundii (1, 2) and Escherichia coli (3). In the forward direction the enzyme catalyzes the formation of polyribonucleotides similar in structural details to natural RNA1 (5-8). In the reverse reaction polyribonucleotides are phosphorolyzed to yield nucleoside diphosphates. The phosphorolysis of synthetic polymers made by the enzyme and the phosphorolysis of ribonucleic acids isolated from various natural sources have been studied by Ochoa and coworkers with the A. VineZundii enzyme (2, 9), by Littauer and Kornberg with a preparation from E. coli (3), and by Heppel.2 Highly polymerized RNA preparations were phosphorolyzed at slower rates than the synthetic polymers; however, commercial RNA and RNA “core,” the limit polynucleotides obtained after exhaustive
منابع مشابه
Polynucleotide phosphorylase of Micrococcus lysodeiktpcus. III. The apparent arsenolysis of nucleoside diphosphates by polynucleotide phosphorylase.
The enzyme, polynucleotide phosphorylase, catalyzes the polymerization of nucleoside diphosphates to polyribonucleotides with the formation of inorganic orthophosphate (1, 2). The reaction is readily reversible, and the phosphorolysis of polyribonucleotides has been studied extensively (3-6). Several recent reviews (7-9) afford extensive summaries of the literature. In the accompanying paper (l...
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We have examined the ability of wild-type polynucleotide phosphorylase (PNPase) from Streptomyces coelicolor and two mutant forms of the enzyme, N459D and C468A, to function in the polymerization of ADP and in the phosphorolysis of RNA substrates derived from the S. coelicolor rpsO-pnp operon. The wild-type enzyme was twice as active in polymerization as N459D and four times as active as C468A....
متن کاملStudy on the structure-function relationship of polynucleotide phosphorylase: model of a proteolytic degraded polynucleotide phosphorylase A.Guissani and C.Portier Institut de Biologie Physico-chimique,
It is already known that modification of E. col i polynucleotide phosphorylase by endogenous proteolysis induces drastic changes in both phosphorolysis and polymerisation reactions. The structural parameters of the proteolysed polynucleotide phosphorylase are described. The phosphorolysis of polynucleotide, which is quite progressive for the native enzyme, is shown to be only partially progress...
متن کاملOligoribonuclease is distinct from the other known exoribonucleases of Escherichia coli.
Oligoribonuclease, an exoribonuclease specific for small oligoribonucleotides, was initially characterized 20 years ago (S. K. Niyogi and A. K. Datta, J. Biol. Chem. 250:7307-7312, 1975) and shown to be different from RNase II and polynucleotide phosphorylase. Here we demonstrate, using mutant strains and purified enzymes, that oligoribonuclease is not a manifestation of RNases D, BN, T, PH, an...
متن کاملThe polymerization of guanosine diphosphate by polynucletide phosphorylase.
Polynucleotide phosphorylase catalyzes the reversible polytion of nucleoside diphosphates (1). With enzyme prepns from Escherichia coli (2), Azotobacter agile (3), and Mius lysodeikticus (4, 5) a reaction has been observed with additions of adenosine, uridine, cytosine, or inosine diphosto form the corresponding homopolymer. However, the erization of guanosine diphosphate represents a special ....
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 232 1 شماره
صفحات -
تاریخ انتشار 1958