Results 151 to 160 of about 16,842 (191)

Mechanism of polynucleotide phosphorylase

Biochemistry, 1989
The de novo polymerization of RNA initiated by polynucleotide phosphorylase from nucleoside diphosphates was examined. End group analysis performed under conditions designed to specifically end label the polymer revealed no evidence for a 5'-pyrophosphate-terminated polymer.
M, Sulewski, S P, Marchese-Ragona, K A, Johnson, S J, Benkovic   +3 more
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Model for the elongation of polynucleotide chains by polynucleotide phosphorylase

Journal of Molecular Biology, 1970
Abstract The experiments described in this paper were designed to elucidate the mechanism of elongation of a polynucleotide chain catalysed by polynucleotide phosphorylase. The problem has been approached in three different ways, essentially: (1) examination of the size distribution of the end products isolated during the course of the reaction; (2 ...
M N, Thang, R A, Harvey, M, Grunberg-Manago   +2 more
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THE MECHANISM OF ACTION OF POLYNUCLEOTIDE PHOSPHORYLASE

Annals of the New York Academy of Sciences, 1959
The purpose of this paper is to review certain aspects of the mechanism of action of polynucleotide phosphorylase and to present, rather briefly, some recent findings. The discussion will be concerned with studies carried out by S. Ochoa and his associates a t New York University, New York, N.
L A, HEPPEL, M F, SINGER, R J, HILMOE
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The origin of polynucleotide phosphorylase domains

Molecular Phylogenetics and Evolution, 2004
In this report, we document the presence of polynucleotide phosphorylase (PNPase) in the animal eukaryotes. These proteins contain several domains, including 2 RNase PH domains (PNPase 1 and PNPase 2) which are closely related functionally and in sequence similarity to ribonuclease PH (RPH) protein.
Magdalena, Leszczyniecka, Rob, DeSalle, Dong-Chul, Kang, Paul B, Fisher   +3 more
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The relationship of mono- and polynucleotide conformation to catalysis by polynucleotide phosphorylase

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1970
Abstract 8-Bromoguanosine 5′-diphosphate, 8-oxoguanosine 5′-diphosphate, 6-methylcytidine 5′-diphosphate and 2,6-quinazoline dione 1′-ribosyl 5′-diphosphate are inactive as substrates for homopolymer synthesis with polynucleotide phosphorylase. They inhibit polymerization and exchange but not phosphorolysis.
A M, Kapuler, C, Monny, A M, Michelson
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Overexpression and purification of untagged polynucleotide phosphorylases

Protein Expression and Purification, 2003
We report here the development of new, straightforward procedures for the purification of bacterial polynucleotide phosphorylases (PNPases). The pnp genes from Streptomyces antibioticus, Streptomyces coelicolor, and Escherichia coli were overexpressed using the vectors pET11 and pET11A in E. coli BL21(DE3)pLysS.
George H, Jones, Martyn F, Symmons, Janet S, Hankins, George A, Mackie   +3 more
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Activation of Polynucleotide Phosphorylase by Salts

Nature, 1957
IN the course of purification studies of polynucleotide phosphorylase (polyase) from M. lysodeikticus we have on several occasions noticed that, after dialysis against buffers at low ionic strength or distilled water, considerable loss of enzyme activity occurred.
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Polynucleotide phosphorylase from plant cells

Plant Cell Reports, 1984
The isolation of polynucleotide phosphorylase (EC 2. 7. 7. 8) from suspension cultured plant cells of parsley (Petroselinum sativum) and from tomato seedlings (Lycopersicon esculentum) is described. The procedure includes an ultracentrifugation step, a glycerol density gradient centrifugation and preparative gel electrophoresis under nondenaturing ...
E, Schumacher-Wittkopf, G, Richter, S, Schulze   +2 more
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Human polynucleotide phosphorylase: location matters

Trends in Cell Biology, 2007
Human polynucleotide phosphorylase (hPNPase) is an RNA-processing enzyme induced in response to type I interferons and during terminal differentiation and cellular senescence. hPNPase was thought to contribute to cellular senescence through its RNA-degrading activity in the cytosol; however, recent studies show that hPNPase localizes to the ...
Hsiao-Wen, Chen, Carla M, Koehler, Michael A, Teitell   +2 more
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Synthesis of polypseudouridylic acid by polynucleotide phosphorylase

Biochimica et Biophysica Acta, 1963
Abstract 1. 1. Polypseudouridylic acid was synthesized in good yield from pseudouridine diphosphate by polynucleotide phosphorylase (EC 2.7.7.8) of Micrococcus lysodeikticus. Primer trinucleotide, pApApA markedly increased the synthetic reaction rate but did not affect the [32P]Pi-pseudouridine diphosphate exchange. 2. 2.
L, SASSE, M, RABINOWITZ, I H, GOLDBERG
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