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Literature summary for 2.7.7.8 extracted from

  • Briani, F.; Del Favero, M.; Capizzuto, R.; Consonni, C.; Zangrossi, S.; Greco, C.; De Gioia, L.; Tortora, P.; Deho, G.
    Genetic analysis of polynucleotide phosphorylase structure and functions (2007), Biochimie, 89, 145-157.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Protein Variants

Protein Variants Comment Organism
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

Organism UniProt Comment Textmining
Escherichia coli
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Escherichia coli P05055
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