However, the enzyme discovered by Ochoa (polynucleotide phosphorylase) was later shown to be responsible for RNA degradation, not RNA synthesis. RNA - Wikipedia While many bacteria and mitochondria have polyadenylate polymerases, they also have another type of polyadenylation, performed by polynucleotide phosphorylase itself.

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FEBS Letters, 1985. Damian Labuda. Download PDF. Download Full PDF Package. This paper. A short summary of this paper. 37 Full PDFs related to this paper. READ PAPER.

Polynucleotide phosphorylase

Although this enzyme can catalyze untemplated RNA synthesis from nucleoside diphosphates, conditions in the cell favor the reverse, degradative reaction. Polynucleotide phosphorylase (PNPase) is an evolutionary conserved 3',5' exoribonuclease, which plays a central role in RNA processing in bacteria and plants. In Severo Ochoa. …named the enzyme he discovered polynucleotide phosphorylase. It was subsequently determined that the enzyme’s function is to degrade RNA, not synthesize it; under test-tube conditions, however, it runs its natural reaction in reverse. The enzyme has been singularly valuable in enabling scientists to understand and re-create the process whereby the…. Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3′ to 5′ exoribonuclease activity and a 3′-terminal oligonucleotide polymerase activity.

Polynucleotide phosphorylase (PNPase) is an evolutionary conserved 3',5' exoribonuclease, which plays a central role in RNA processing in bacteria and plants.

Tyrosine kinase 2 - Wikipedia. Autophosphorylation - Wikipedia. Protein kinase domain - Wikipedia.

Polynucleotide Phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. That is, it dismantles the RNA chain starting at the 3' end and working toward the 5' end. It also synthesizes long, highly heteropolymeric tails in vivo.

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.

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. 1. Tanpakushitsu Kakusan Koso. 1972 Oct:Suppl:183-8. [Polynucleotide phosphorylase]. [Article in Japanese] Matsuo K, Higuchi S, Tsuboi M. PMID: Polynucleotide phosphorylase is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. It is involved on mRNA processing and degradation in bacteria, plants, and in humans.
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The role of PNPase is pleiotropic. As orthologs of the two major ribonucleases (RNase E and RNase II) of Escherichia coli are missing in the Campylobacter jejuni genome, in the current study the focus has been on the C. jejuni POLYNUCLEOTIDE PHOSPHORYLASE (PNPase) 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).

Based on sequence analysis and catalytic 61610 Int.Cl.6 C07H 21/00;C12N 9/12. PREPARATION OF POLYNUCLEOTIDES. USING PURIFIED POLYNUCLEOTIDE PHOSPHORYLASE.
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Repair of the 3′-terminal -CCA sequence of tRNA generally requires the action of the enzyme tRNA nucleotidyltransferase. However, in Escherichia coli in the absence of this enzyme, a decreased level of tRNA end repair continues. To ascertain the enzymes responsible for this residual repair, mutant strains were constructed lacking tRNA nucleotidyltransferase and other enzymes potentially

Acad. 2002 Sci. USA. 99:8784-9. Koch-Nolte Polyribonucleotide Nucleotidyltransferase. engelska.