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Literature summary for 3.1.13.1 extracted from

  • Amblar, M.; Barbas, A.; Fialho, A.M.; Arraiano, C.M.
    Characterization of the functional domains of Escherichia coli RNase II (2006), J. Mol. Biol., 360, 921-933.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of a large set of RNase II truncated proteins and comparison of them to the wild-type regarding their exoribonucleolytic activity and RNA-binding ability. The dissociation constants are determined using different single- or double-stranded substrates. The results obtained reveal that S1 is the most important domain in the establishment of stable RNA–protein complexes, and its elimination results in a drastic reduction on RNA-binding ability. The N-terminal CSD plays a very specific role in RNase II, preventing a tight binding of the enzyme to single-stranded poly(A) chains. The biochemical results obtained with a mutant that lacks both putative RNA-binding domains, reveals the presence of an additional region involved in RNA binding. Such region, is identified by sequence analysis and secondary structure prediction as a third putative RNA-binding domain located at the N-terminal part of RNB catalytic domain Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oligonucleotide + H2O
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Escherichia coli ?
-
?
poly(A) + H2O
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Escherichia coli ?
-
?