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Literature summary extracted from

  • Unciuleac, M.C.; Shuman, S.
    Discrimination of RNA from DNA by polynucleotide phosphorylase (2013), Biochemistry, 52, 6702-6711.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.8 D526A mutation of the full-length and S1-domain deletion PNPases does not affect manganese- or magnesisum-dependent binding to RNA Mycolicibacterium smegmatis
2.7.7.8 D526A/D532A mutation of the full-length and S1-domain deletion PNPases does not affect manganese-or magnesium-dependent binding to RNA Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.8 Mg2+ substituting manganese for magnesium as the metal cofactor enables PNPase to nibble into the DNA tract. A 3'-phosphate group prevents RNA phosphorolysis when the metal cofactor is magnesium Mycolicibacterium smegmatis
2.7.7.8 Mn2+ with manganese as metal cofactor, PNPase can resect an RNA 3'-phosphate end, albeit 80fold slower than a 3'-OH Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.8 Mycolicibacterium smegmatis A0QVQ5
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-

Synonyms

EC Number Synonyms Comment Organism
2.7.7.8 PNPase
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 Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
2.7.7.8 physiological function PNPase discriminates RNA versus DNA during the 3' phosphorolysis reaction. A kinetic block to 3' phosphorolysis of a DNA tract within an RNA polynucleotide is exerted when resection has progressed to the point that a 3' monoribonucleotide flanks the impeding DNA segment. The position of the pause one nucleotide upstream of the first deoxynucleotide encountered is independent of DNA tract length. The duration of the pause is affected by DNA tract length, being transient for a single deoxynucleotide and durable when two or more consecutive deoxynucleotides are encountered Mycolicibacterium smegmatis