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Literature summary for 2.7.7.8 extracted from

  • Salvo, E.; Alabi, S.; Liu, B.; Schlessinger, A.; Bechhofer, D.H.
    Interaction of Bacillus subtilis polynucleotide phosphorylase and RNase Y: structural mapping and effect on mRNA turnover (2016), J. Biol. Chem., 291, 6655-6663.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of structure based on Escherichia coli PNPase crystal structure. Residues Glu20, Arg35, Asp323, Glu331, and Arg546 are hypothesized to be involved in the RNase Y interaction Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
D323A weakening of interaction with RNase Y. Asp-323 sits near the C-terminal end of the RNase Y peptide sequence Bacillus subtilis
E331A loss of interaction with RNase Y. The Glu-331 side faces the helical domain of the RNase Y peptide Bacillus subtilis
R35A weakening of interaction with RNase Y. The Arg35 side chain faces the non-helical domain of the binding peptide Bacillus subtilis
R546A weakening of interaction with RNase Y. Arg546 is located farther away from the binding peptide Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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Bacillus subtilis BG1
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General Information

General Information Comment Organism
physiological function mutations in PNPase residues predicted to be involved in RNase Y binding show a loss of PNPase-RNase Y interaction. For the two mRNAs investigated, disruption of the PNPase-RNase Y interaction does not appear to affect mRNA turnover Bacillus subtilis