A novel RNA digesting activity from commercial polynucleotide phosphorylase
نویسندگان
چکیده
منابع مشابه
From polynucleotide phosphorylase to neurobiology.
In the fall of 1944, I enrolled at the Hebrew University of Jerusalem. The student body numbered about 700 and the choice of faculties was somewhat limited.My hopewas to study medicine, but the plans to open a medical school were still at the drawing board stage. I therefore chose to study chemistry with biochemistry and bacteriology as minor subjects, which I thought I would need later if I we...
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We have isolated cDNA clones encoding a novel RNAbinding protein that is a component of a multisubunit poly(A) polymerase from pea seedlings. The encoded protein bears a significant resemblance to polynucleotide phosphorylases (PNPases) from bacteria and chloroplasts. More significantly, this RNA-binding protein is able to degrade RNAs with the resultant production of nucleotide diphosphates, a...
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Polynucleotide phosphorylase (PNPase), a 3' to 5' exonuclease encoded by pnp, plays a key role in Escherichia coli RNA decay. The enzyme, made of three identical 711 amino acid subunits, may also be assembled in the RNA degradosome, a heteromultimeric complex involved in RNA degradation. PNPase autogenously regulates its expression by promoting the decay of pnp mRNA, supposedly by binding at th...
متن کاملIsolation and characterization of a polynucleotide phosphorylase from Bacillus amyloliquefaciens.
Bacillus amyloliquefaciens BaM-2 produces large amounts of extracellular enzymes, and the synthesis of these proteins appears to be dependent upon abnormal ribonucleic acid metabolism. A polynucleotide phosphorylase (nucleoside diphosphate:polynucleotide nucleotidyl transferase) was identified, purified, and characterized from this strain. The purification scheme involved cell disruption, phase...
متن کاملA deoxyadenylate kinase activity associated with polynucleotide phosphorylase from Micrococcus luteus.
We report here the presence of two enzymatic activities associated with highly purified preparations of polynucleotide phosphorylase from Micrococcus luteus. The first, a nuclease activity, which is not separated from the phosphorylase on hydroxylapatite, may be due to substitution of H2O for phosphate in the phosphorolysis reaction. The second activity, a deoxyadenylate kinase, the bulk of whi...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1985
ISSN: 0014-5793
DOI: 10.1016/0014-5793(85)80520-2