PMO - PolyMetylenoxid; PNPA - PolyNucleotide Phosphorylase A; PNPB - PolyNucleotide Phosphorylase B; Po - Polonium; POC - Polar

comR (pnpA) is a newly identified gene in Bacillus subtilis that is necessary for the expression of late competence genes. Transformability of a comR (pnpA) mutant is 1–5% of that seen in comR + strains. Cloning and sequencing identified ComR as polynucleotide phosphorylase (PNPase).

(2001) Biochemistry 40, 9977 polyribonucleotide nucleotidyltransferase: ( pol'ē-rī'bō-nū'klē-ō-tīd nū'klē-o-tīd'il-trans'fĕr-ās ), An enzyme-catalyzing phosphorolysis of polyribonucleotides or of RNA, yielding nucleoside diphosphates (or the reverse, the first artificial polynucleotide formation discovered). Synonym(s): polynucleotide phosphorylase Polynucleotide phosphorylase 1 ARBA annotation (EC: 2.7.7.8 ARBA annotation) Organism i: Danio rerio (Zebrafish) (Brachydanio rerio) Imported. Taxonomic identifier i Polynucleotide phosphorylase, RNase II and RNase E play different roles in the in vivo modulation of polyadenylation in Escherichia coli Bijoy K. Mohanty Department of Genetics, University of Georgia, Athens, GA 30605, USA. polynucleotide phosphorylase (PNPase) was isolated from a chloroplast protein extract and found to be the protein respon-sible for most exoribonucleolytic activity. The homology of the chloroplast and the bacterial enzymes was observed both in amino acid sequences and in biochemical characteristics (20).

WADE HE, LOVETT S. The Biochemical Journal, 01 Nov 1961, 81: 319-328 DOI: 10.1042 Nostoc polynucleotide phosphorylase 2047 were sealed into plastic bags with 100 ml incubation mixtures consisting of CAPS buffer, 10 ~M-ADP and, when required, 0.05 mg ml-I poly(U) as primer. The Polyguanylic acid (poly(G)) was synthesized from GDP in a yield of 60-75% by Thermus thermophilus polynucleotide phosphorylase (polyribonucleotide: orthophosphate nucleotidyltransferase, EC 2.7.7.8) at 70°C, pH 8.5 in the presence of Mg 2+. Neisseria meningitidis autoaggregation is an important step during attachment to human cells. Aggregation is mediated by type IV pili and can be modulated by accessory pilus proteins, such as PilX, and posttranslational modifications of the major pilus subunit PilE. The mechanisms underlying the regulation of aggregation remain poorly characterized. Polynucleotide phosphorylase (PNPase) is a 3 Aug 27, 2013 Polynucleotide phosphorylase(1) (PNPase) catalyzes stepwise phosphorolysis of the 3′-terminal phosphodiesters of RNA chains to yield Polynucleotide phosphorylase from Synechocystis sp. (PNPase ); Escherichia coli; Polynucleotide phosphorylase has been used in a study to discover that a Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a 3′- terminal oligonucleotide polymerase activity and a phosphorolytic 3′ to 5′.

Widely distributed among bacteria and eukaryotes, including humans, polynucleotide phosphorylase (PNPase) is a critical enzyme in RNA metabolism that functions in most organisms as a 3ʹ to 5ʹ exoribonuclease.

nucleic acids res. was also helpful in polymerising RNA with defined sequences in a template independent manner. 1.

Polynucleotide Phosphorylase PNP was discovered in 1955 by Marianne Grunberg-Manago and Severo Ochoa (Ochoa shared the Noble Prize with Arthur

keywords = "RPSO MESSENGER-RNA, POLY(A) POLYMERASE I, POLYNUCLEOTIDE PHOSPHORYLASE, POLY(A)-DEPENDENT DEGRADATION, Rnase ph: an escherichia coli phosphate-dependent nuclease distinct from polynucleotide phosphorylase.Final trimming of the 3' terminus of tRNA precursors in His discoveries include the first cloning of p21 (CDK inhibitor), human polynucleotide phosphorylase, mda-9/syntenin (a pro-metastatic gene), mda-5 and Medicine had been awarded to Severo Ochoa for the discovery of what was believed to be RNAP, but instead turned out to be polynucleotide phosphorylase.

Polyguanylic acid (poly(G)) was synthesized from GDP in a yield of 60-75% by Thermus thermophilus polynucleotide phosphorylase (polyribonucleotide: orthophosphate nucleotidyltransferase, EC 2.7.7.8) at 70°C, pH 8.5 in the presence of Mg 2+. Polynucleotide Phosphorylase: In 1955, Marianne Grunberg-Manago and Severo Ochoa reported the isolation of an enzyme that catalyzed the synthesis of RNA. Dec 1, 2007 Human polynucleotide phosphorylase (hPNPase) is an RNA-processing enzyme induced in response to type I interferons and during terminal Aug 27, 2013 Polynucleotide phosphorylase(1) (PNPase) catalyzes stepwise phosphorolysis of the 3′-terminal phosphodiesters of RNA chains to yield Polynucleotide phosphorylase from Synechocystis sp. (PNPase ); Escherichia coli; Polynucleotide phosphorylase has been used in a study to discover that a Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a 3′- terminal oligonucleotide polymerase activity and a phosphorolytic 3′ to 5′. Polynucleotide phosphorylase is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase Apr 1, 2012 Polynucleotide phosphorylase (PNPase) is an exoribonuclease that cleaves single-stranded RNA substrates with 3′–5′ directionality and Dec 14, 2007 Polynucleotide phosphorylase (PNPase) (EC 2.7.7.8) was the first enzyme to be identified that catalyzes the formation of polynucleotides from Aug 22, 2011 Abstract.
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Widely distributed among bacteria and eukaryotes, including humans, polynucleotide phosphorylase (PNPase) is a critical enzyme in RNA metabolism that functions in most organisms as a 3ʹ to 5ʹ exoribonuclease.

Polynucleotide phosphorylase is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase Apr 1, 2012 Polynucleotide phosphorylase (PNPase) is an exoribonuclease that cleaves single-stranded RNA substrates with 3′–5′ directionality and Dec 14, 2007 Polynucleotide phosphorylase (PNPase) (EC 2.7.7.8) was the first enzyme to be identified that catalyzes the formation of polynucleotides from Aug 22, 2011 Abstract. Bacillus subtilis pnpA gene product, polynucleotide phosphorylase ( PNPase), is involved in double-strand break (DSB) repair via Polynucleotide Phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide The enzyme Polynucleotide Phosphorylase polymerizes individual rNDP molecules as a poly-RNA molecule. This provides an artificial messenger RNA for in Polynucleotide Polynucleotide Phosphorylase (PNPase) plays important roles in mRNA processing and degradation in various cells.
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Recollections on studies of polynucleotide phosphorylase:a commentary on ‘Enzymic synthesis of polynucleotides. I. Polynucleotide phosphorylase of Azobacter vinelandii’ by M. Grunberg-Manago, P.J. Ortiz and S. Ochoa Biochim. Biophys. Acta 20 (1956) 269–285. Biochimica et Biophysica Acta (BBA) - General Subjects 1989, 1000 , 59-81.

The homology of the chloroplast and the bacterial enzymes was observed both in amino acid sequences and in biochemical characteristics (20). To gain novel insights on mechanism regulating fengycin production, we investigated the effect of the fascinating polynucleotide phosphorylase (PNPase), as well as the effect of lipopeptide surfactin. Polynucleotide phosphorylase (EC 2.7.7.8).

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Polynucleotide phosphorylase from Synechocystis sp. (PNPase ); Escherichia coli; Polynucleotide phosphorylase has been used in a study to discover that a

It also synthesizes long, highly heteropolymeric tails in vivo. RNase E nucleates assembly of a complex, designated the RNA degradosome, that includes polynucleotide phosphorylase (PNPase, a 3′–5′ exoribonuclease), an ATP-dependent RNA helicase (RhlB), and enolase (a metabolic enzyme that may serve as a scaffold); poly (A) polymerase is also associated with the complex. Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3′ to 5′ exoribonuclease activity and a 3′-terminal oligonucleotide polymerase activity. It is also involved in mRNA processing and degradation in bacteria, plants, and humans. Physical form Polynucleotide phosphorylase promotes the stability and function of Hfq-binding sRNAs by degrading target mRNA-derived fragments. Inhibition of homologous PNPase by citrate may represent an evolutionarily conserved communicative link between RNA degradation and central metabolism.