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Literature summary for 2.7.7.8 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
Search for more literature for 2.7.7.8

Protein Variants

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

Metals/Ions Comment Organism Structure
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
Mn2+ with manganese as metal cofactor, PNPase can resect an RNA 3'-phosphate end, albeit 80fold slower than a 3'-OH Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0QVQ5
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Synonyms

Synonyms Comment Organism
PNPase
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 Mycolicibacterium smegmatis

General Information

General Information Comment Organism
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