Cloned (Comment) | Organism |
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Escherichia coli |
Protein Variants | Comment | Organism |
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A552T | complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance | Escherichia coli |
A552T | ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.7, as compared with 1.0 in wild-type | Escherichia coli |
DELTA549-709 | complementation of growth defect at 15°C of host strain | Escherichia coli |
E371K | complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance | Escherichia coli |
E371K | ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type | Escherichia coli |
E81D | complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity | Escherichia coli |
E81D | impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 1.6, as compared with 1.0 in wild-type | Escherichia coli |
E81K | complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity | Escherichia coli |
E81K | impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.4, as compared with 1.0 in wild-type | Escherichia coli |
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 | Escherichia coli |
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 | Escherichia coli |
P98L | impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.03, as compared with 1.0 in wild-type | Escherichia coli |
R97C | complementation of growth defect at 15°C of host strain. Severe reduction of enzyme activity and increased PNPase expression levels | Escherichia coli |
R97C | ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.1, as compared with 1.0 in wild-type | Escherichia coli |
V304A/V305D | complementation of growth defect at 15°C of host strain | Escherichia coli |
V304A/V305D | ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.02, as compared with 1.0 in wild-type | Escherichia coli |
V521I | complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance | Escherichia coli |
V521I | ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.5, as compared with 1.0 in wild-type | Escherichia coli |
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 | Escherichia coli |
V639D | impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type | Escherichia coli |
W233Stop | complementation of growth defect at 15°C of host strain | Escherichia coli |
Organism | UniProt | Comment | Textmining |
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Escherichia coli | - |
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Escherichia coli | P05055 | - |
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