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	
2.7.7.8	D625N	naturally occuring mutation in the catalytic site, inactive mutant	-, 723424	
2.7.7.8	DELTA549-709	complementation of growth defect at 15°C of host strain	672449	
2.7.7.8	E331A	loss of interaction with RNase Y. The Glu-331 side faces the helical domain of the RNase Y peptide	-, 738702	
2.7.7.8	E371K	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	E371K	ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type	672449	
2.7.7.8	E81D	complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity	672449	
2.7.7.8	E81D	impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 1.6, as compared with 1.0 in wild-type	672449	
2.7.7.8	E81K	complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity	672449	
2.7.7.8	E81K	impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.4, as compared with 1.0 in wild-type	672449	
2.7.7.8	F635A	site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme	722555	
2.7.7.8	F635A/F638A/H650A	site-directed mutagenesis, the mutant enzyme shows highly reduced activity and an increased RNA binding constant compared to the wild-type enzyme	722555	
2.7.7.8	F635R/F638R/H650R	site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme	722555	
2.7.7.8	F638A	site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme	722555	
2.7.7.8	G1307A	mutation invovled in sRNA regulation defects	-, 723757	
2.7.7.8	G1466A	mutation invovled in sRNA regulation defects	723757	
2.7.7.8	G570C	site-directed mutagenesis, the mutant enzyme shows highly reduced activity and an increased RNA binding constant compared to the wild-type enzyme	722555	
2.7.7.8	G570C/V679A	site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme	722555	
2.7.7.8	G596R	naturally occuring mutation near the catalytic domain, inactive mutant. Mutant G596R fails to fold correctly, perhaps as a consequence of its inability to bind phosphate, and is thus marked for degradation	-, 723424	
2.7.7.8	G622D	site-directed mutagenesis	723295	
2.7.7.8	H650A	site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme	722555	
2.7.7.8	I555T	site-directed mutagenesis, the mutant enzyme shows slightly reduced activity compared to the wild-type enzyme	722555	
2.7.7.8	I576A	site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme	722555	
2.7.7.8	I576A/F638A	site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme	722555	
2.7.7.8	I576T	site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme	722555	
2.7.7.8	I576T/F638A	site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme	722555	
2.7.7.8	I576T/T585A	site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme	722555	
2.7.7.8	K571L	site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme	722555	
2.7.7.8	K571Q	site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme	722555	
2.7.7.8	additional information	C-terminal KH/S1 domain truncated mutant, crystallization data. Mutant binds and cleaves RNA less efficiently with an 8fold reduced binding affinity and forms a less stable trimer. Mutation of Arg-residues in the central channel neck region produces defective enzymes that either bind and cleave RNA less efficiently or generate longer cleaved oligonucleotide products	690030	
2.7.7.8	additional information	construction of a pnp inactivation mutant, comparative proteomic analysis and 81-176 phenotype, overview. Levels of peb3 and katA mRNA are significantly decreased in the pnp mutant strain compared to the parental strain, while gene expression of luxS and hsp90 remains unaffected by the pnp mutation, but not protein expression, overview. Poly(A) degradation by lysates of the pnp mutant strain is almost totally non-responsive to phosphate addition	722312	
2.7.7.8	additional information	construction of a strain in which PNPase activity is uncoupled from the degradosome through the deletion of the C-terminal degradosome-scaffold-ing domain of RNase E. Compared with the parental strain, significant differences are distributed across many metabolic pathways, including the Krebs cycle, amino acid synthesis, and glycolysis in the mutant strain. Salient differences are seen for amino acids and increases in the concentrations of succinate, fumarate, and malate, suggesting uncoupling of the two halves of the Krebs cycle	-, 722702	
2.7.7.8	additional information	construction of domain deletion mutants DELTAKH DELTAS1, DELTAKH, and DELTAS1	722555	
2.7.7.8	additional information	construction of gene pnp deletion mutants, the mutants do not exhibit cold sensitivity, phenotype, overview	-, 680444	
2.7.7.8	additional information	construction of hybrid proteins by replacing the S1 RNA binding domain of RNase II for the S1 from enzyme. PNPase S1 domain can partially restore the RNA-binding ability and exonucleolytic activity of Rnase II and is able to induce the trimerization of the Rnase II-PNPase hybrid protein	677105	
2.7.7.8	additional information	deletion of gene pnp in Eschericchia coli strain C-1a leading to strong cell aggregation in liquid medium dependent on the extracellular polysaccharide poly-N-acetylglucosamine. Operon pgaABCD transcript levels are increased in the pnp mutant compared to the wild-type enzyme. Inactivation of the pnp gene induces poly-N-acetylglucosamine production. The aggregative phenotype of the C-5691 (DELTApnp) strain is complemented by basal expression from a multicopy plasmid of the pnp gene under araBp promoter, overview	-, 721941	
2.7.7.8	additional information	deletion of KHS1 domain, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type. Deletion mutant lacking amino acids 549-709, no growth at 15°C. Both first and second core domains are involved in the catalysis of the phosphorolytic reaction, and both phosphorolytic activity and RNA binding are required for autogenous regulation and growth in the cold	672449	
2.7.7.8	additional information	depletion of enzyme by RNAi approach or overexpression of c-myc protects melanoma cells from interferon-beta mediated grwoth inhibition. Targeted overexpression of enzyme as a therapeutic strategy for c-myc overexpressing and interferon-beta resisitant tumors	672972	
2.7.7.8	additional information	enzyme deletion strain is less virulent in mouse than the isogenic wild-type. Enzyme deletion strains show enhanced levels of type III secretion system T3SS encoding transcripts and proteins. T3SS expression levels do not differ between enzyme deletion strains expressing active and inactive S1 RNA binding domain of enzyme which is required for normal T3SS activity	673749	
2.7.7.8	additional information	enzyme depletion using RNAi does not affect mitochondrial RNA levels but impairs mitochondrial electrochemical membrane potential, decreases respiratory chain activity and correlates with altered mitochondrial morphology. This results in F0F1-ATP synthase instability, impaired ATP generation, lactate accumulation, and AMP kinase phosphorylation with reduced cell proliferation	675974	
2.7.7.8	additional information	enzyme inactivation strain, PNPase deficiency results in increased expression of salmonella plasmid virulence genes. Six genes are significantly upregulated, including spvABC, rtcB, entC, and STM2236. A growth advantage of the mutant strain in BALB/c mice depends on plasmid virulence gene spvR as well	673983	
2.7.7.8	additional information	expression of polynucleotide phosphorylase mutants lacking specific functional domains, i.e., mitochondrial translocation signal (MTS), catalytic domains (RPH1 and RPH2) and RNA binding domains (KH and S1), in cultured HeLa cells. MTS is required for polynucleotide phosphorylase to reduce 8-hydrooxyguanosine in mitochondria, but not in cytoplasm. Both RPH1 or RPH2 domain alone are able to support the full activity of polynucleotide phosphorylase in reducing 8-hydrooxyguanosine during oxidative stress, and the S1 RNA-binding domain, but not KH, is required for polynucleotide phosphorylase to reduce 8-hydrooxyguanosine under oxidative stress	761251	
2.7.7.8	additional information	generation of a S1 domain-lacking mutant enzyme, domain organization of full-length and S1 domain-truncated hPNPase. overview. Full-length and DELTAS1 hPNPase cleave the poly(A)12 and poly(U)12 RNA with similar activities and DELTAS1 hPNPase cleaves ssRNA substrate almost as efficiently as full-length PNPase	723295	
2.7.7.8	additional information	genetic selection and screen for mutants defective in the post-transcriptional regulation of gene expression by sRNAs, i.e. CyaR, SgrS, and RyhB. Each of the pnp mutations isolated, as well as a pnp deletion, are transduced into strain DJ624, overview. The defect in sRNA regulation caused by the pnp mutations is independent of Hfq. While Hfq does not appear to be limiting, it seems possible that lack of PNPase leads to inactivation of Hfq	-, 723757	
2.7.7.8	additional information	human melanoma cells are infected with empty adenovirus or with an adenovirus expressing hPNPaseold-35 and identification of miRNAs differentially and specifically regulated by hPNPaseold-35	723628	
2.7.7.8	additional information	in a mutant lacking polyribonucleotide phosphorylase activity, the pattern of outer membrane proteins is changed. In stationary phase, stationary phase regulator MicA RNA levels are increased in the mutant, leading to a decrease in the levels of its target ompA mRNA and the respective protein	-, 695112	
2.7.7.8	additional information	overexpression of polynucleotide phosphorylase in HeLa cells under oxidative stress conditions reduces RNA oxidation and increases cell viability against H2O2 insult. Knock-down of enzyme decreases viability and increases 8-oxoguanosine levels in cells exposed to H2O2	690735	
2.7.7.8	additional information	polynucleotide phosphorylase deletion strain is less virulent in mouse compared with the isogenic wild-type strain. Deletion strains possess enhanced levels of type III secretion system-encoding transcripts and proteins. A S1 variant of polynucleotide phosphorylase containing a disruption in its RNA-binding subdomain cannot restore normal type III secretion system activity	673749	
2.7.7.8	additional information	several new pnp alleles constructed. To identify specific cis-acting determinants of PNPase autoregulation and discriminate between the two proposed models, several pnpL DELTApnp-871 mutants and one DELTApnp-1010t DELTApnp-871 chromosomal double mutant are constructed	692896	
2.7.7.8	additional information	stable silencing by establishing HeLa cell lines expressing shRNA. Silencing significantly affects processing and polyadenylation of mitochondrial mRNAs with different effects on different genes. The stable poly(A) tails at the 3' ends of COX1 transcripts are abolished, while COX3 poly(A) tails remain unaffected and ND5 and ND3 poly(A) extensions increase in length. Despite the lack of polyadenylation at the 3' end, COX1 mRNA and protein accumulate to normal levels, as is the case for all 13 mitochondria-encoded proteins. ATP depletion also alters poly(A) tail length	695110	
2.7.7.8	additional information	study on the effect of specific mutations in the two RNA binding domains KH and S1. Removal of critical motifs that stabilize the hydrophobic core of each domain, as well as a complete deletion of both severely impaireds binding to RNA. all mutants are enzymatically active but display significant changes in the kinetic behaviour of both phosphorolysis and polymerization activities. Mutants do not autoregulate efficiently and are unable to complement the growth defect of a chromosomal enzmye deletion at 18°C	691041	
2.7.7.8	additional information	targeted overexpression of hPNPase represents a strategy to selectively downregulate RNA expression and consequently intervene in a variety of pathophysiological conditions, enzyme silencing in PNPase RNA interference-transfected HEK293 cells	723310	
2.7.7.8	additional information	the promoter of Progression Elevated Gene-3 functions selectively in a diverse array of human cancer cells. An adenovirus constructed with the Progression Elevated Gene-3 promoter driving expression of polyribonucleotide phosphorylase containing a C-terminal hemaglutinin-tag induces robust transgene expression, growth suppression, apoptosis, and cell-cycle arrest in a broad panel of pancreatic cancer cells	693326	
2.7.7.8	additional information	upon expression in Escherichia coli, human enzyme does not form hetero-complexes with Escheichia coli enzyme	695109	
2.7.7.8	P98L	complementation of growth defect at 15°C of host strain, forms of smaller colonies than host strain. Severe reduction of enzyme activity and increased PNPase expression levels	672449	
2.7.7.8	P98L	impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.03, as compared with 1.0 in wild-type	672449	
2.7.7.8	R100D	growth at 37°C, not able to grow at 15°C	-, 692872	
2.7.7.8	R153A/R372A/R405A/R409A	site-directed mutagenesis	-, 722702	
2.7.7.8	R319H	growth at 37°C, not able to grow at 15°C	-, 692872	
2.7.7.8	R35A	weakening of interaction with RNase Y. The Arg35 side chain faces the non-helical domain of the binding peptide	-, 738702	
2.7.7.8	R398D/R399D	growth at 37°C, not able to grow at 15°C	-, 692872	
2.7.7.8	R546A	weakening of interaction with RNase Y. Arg546 is located farther away from the binding peptide	-, 738702	
2.7.7.8	R83A	the mutation has little apparent effect on activity but causes the full-length PNPase to stall on RNA oligomers shorter than eight nucleotides	693689	
2.7.7.8	R97C	complementation of growth defect at 15°C of host strain. Severe reduction of enzyme activity and increased PNPase expression levels	672449	
2.7.7.8	R97C	ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.1, as compared with 1.0 in wild-type	672449	
2.7.7.8	S441A	catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure	-, 760484	
2.7.7.8	S442A	catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure	-, 760484	
2.7.7.8	S443A	catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure	-, 760484	
2.7.7.8	V304A/V305D	complementation of growth defect at 15°C of host strain	672449	
2.7.7.8	V304A/V305D	ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.02, as compared with 1.0 in wild-type	672449	
2.7.7.8	V521I	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	V521I	ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.5, as compared with 1.0 in wild-type	672449	
2.7.7.8	V639D	complementation of growth defect at 15°C of host strain, migrates slower than wild-type on SDS-PAGE, forms of smaller colonies than host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity	672449	
2.7.7.8	V639D	impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type	672449	
2.7.7.8	W233Stop	complementation of growth defect at 15°C of host strain	672449