Literature summary for 3.1.26.3 extracted from

Paudyal, S.; Alfonso-Prieto, M.; Carnevale, V.; Redhu, S.; Klein, M.; Nicholson, A.
Combined computational and experimental analysis of a complex of ribonuclease III and the regulatory macrodomain protein, YmdB (2015), Proteins, 83, 459-472 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene rnc, phylogenetic analysis, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D128A	site-directed mutagenesis, the D128A mutation in both RNase III subunits, D128A/D128'A, causes an 83fold increase in KD in the interaction of RNase III with YmdB	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A7Y0	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography	Escherichia coli

Synonyms

Synonyms	Comment	Organism
Ec-RNase III	-	Escherichia coli
RNase III	-	Escherichia coli

General Information

General Information	Comment	Organism
malfunction	the YmdB R40A mutation causes a 16fold increase in KD, and the D128A mutation in both RNase III subunits (D128A/D1280A) causes an 83fold increase in KD	Escherichia coli
additional information	complex formation of ribonuclease III with the regulatory macrodomain protein, YmdB, protein-protein docking and interaction analysis by homology modelling (using the Escherichia coli RNase III homodimer as template, PDB entry 1SPV, 2.0 A resolution) and surface plasmon resonance (SPR) analysis, kinetic and thermodynamic values for the YmdB-RNase III interaction, and the effect of specific mutations, overview. Interaction of the conserved YmdB residue R40 with specific RNase III residues at the subunit interface	Escherichia coli

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Release 2023.1 (January 2023)