Results 201 to 210 of about 43,981 (239)
Some of the next articles are maybe not open access.
Mechanism of polynucleotide phosphorylase
Biochemistry, 1989The 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.
Silvio P. Marchese-Ragona +3 more
openaire +3 more sources
THE MECHANISM OF ACTION OF POLYNUCLEOTIDE PHOSPHORYLASE
Annals of the New York Academy of Sciences, 1959The 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.
Maxine F. Singer +2 more
openaire +2 more sources
Model for the elongation of polynucleotide chains by polynucleotide phosphorylase
Journal of Molecular Biology, 1970Abstract 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. Grunberg-Manago +2 more
openaire +3 more sources
Polynucleotide Phosphorylase and the T3SS
2007Low temperatures as well as encounters with host phagocytes are two stresses that have been relatively well studied in many species of bacteria. The exoribonuclease polynucleotide phosphorylase (PNPase) has previously been shown to be required by several species of bacteria, including Yersinia, for low-temperature growth. We have shown that PNPase also
Kurt Schesser, Jason A. Rosenzweig
openaire +3 more sources
Photometric Assay for Polynucleotide Phosphorylase
Analytical Biochemistry, 1999Polynucleotide phosphorylase (PNPase) is a prokaryotic enzyme that catalyzes phosphorolysis of polynucleotides with release of NDPs. It is also believed to play a key role in turnover of prokaryotic transcripts, thus regulating gene expression. At the moment, only radioisotopic methods are available for assaying PNPase in crude extracts; these involve ...
Rebecca Favaro +5 more
openaire +3 more sources
The origin of polynucleotide phosphorylase domains
Molecular Phylogenetics and Evolution, 2004In 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.
Rob DeSalle +3 more
openaire +2 more sources
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. Michelson, C. Monny, A.M. Kapuler
openaire +3 more sources
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. Michelson, C. Monny, A.M. Kapuler
openaire +3 more sources
17 Polynucleotide Phosphorylase
1982Publisher Summary Polynucleotide phosphorylase (PNPase) is the first enzyme that can catalyze the formation of polyribonucleotides with a 3′,5′-phosphodiester bond. In the forward reaction, long polyribonucleotides are synthesized from various ribonucleoside diphosphates, with elimination of inorganic orthophosphate.
H. Soreq, U.Z. Littauer
openaire +2 more sources
Synthesis of polypseudouridylic acid by polynucleotide phosphorylase
Biochimica et Biophysica Acta, 1963Abstract 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.
Irving H. Goldberg +2 more
openaire +3 more sources
18 Polynucleotide Phosphorylase
1972Publisher Summary Polynucleotide phosphorylase (polyribonucleotide : orthophosphate nucleotidyltransferase) designated as PNPase was the first polynucleotide synthesizing enzyme to be discovered. It catalyzes the reversible polymerization of ribonucleoside diphosphates with release of inorganic phosphate. The product of PNPase synthesis is chemically
M. Grunberg-Manago, T. Godefroy-Colburn
openaire +2 more sources