2.7.7.8	A552T	complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance	672449	
2.7.7.8	A552T	ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.7, as compared with 1.0 in wild-type	672449	
2.7.7.8	C1310T	mutation invovled in sRNA regulation defects	-, 723757	
2.7.7.8	C277T	mutation invovled in sRNA regulation defects	-, 723757	
2.7.7.8	C943T	mutation invovled in sRNA regulation defects	-, 723757	
2.7.7.8	D135G	unlike trimeric wild-type, mutant is monomeric. Almost complete inhibition of degradation and polyadenylation activities	695109	
2.7.7.8	D323A	weakening of interaction with RNase Y. Asp-323 sits near the C-terminal end of the RNase Y peptide sequence	-, 738702	
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	737684	
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	737684	
2.7.7.8	D544G	decrease in degradation activity, increase in polymerization	695109