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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Bacillus subtilis BG1 | - |
- |
- |
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 |