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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endonucleolytic cleavage to a 5'-phosphomonoester
catalytic mechanism, overview. The enzyme activates water as a nucleophile to hydrolyze target site phosphodiesters, creating 3'-hydroxyl, 5'-phosphomonoester product termini
RNA 5, a 30 base stem-loop RNA of the sequence 5 '-AUAAAGGUCAUUCGCAAGAGUGGCCUUUAU-3', is cleaved by RNase III (D44N) from Aquifex aeolicus. The products of the reaction include a dinucleotide 5'-AU-3' and a 28 base stem-loop RNA with a two-base 3' overhang (RNA 6). Two RNA 6 molecules and a dimeric mutant enzyme D44N molecule form a product complex
reshaping of fully or partially double-stranded RNA precursors in to mature RNAs involved in pre-mRNA splicing, RNA modification, translation, gene silencing, and regulation of developmental timing
cleavage of fully or partially double-stranded RNA precursors into mature structural and catalytic RNAs such as the snRNAs that splice pre-mRNA, rRNAs, and tRNAs that function in translation, swnoRNAs that guide modification of rRNAs, and individual mRNAs, whose expression they regulate
small hairpins based on the stem structures associated with the Aquifex 16S and 23S rRNA precursors are cleaved at sites that are consistent with production of the immediate precursors to the mature rRNAs. Substrate reactivity is independent of the distal box sequence, but is strongly dependent on the proximal box sequence. RNase III mechanism of dsRNA cleavage, overview
reshaping of fully or partially double-stranded RNA precursors in to mature RNAs involved in pre-mRNA splicing, RNA modification, translation, gene silencing, and regulation of developmental timing
small hairpins based on the stem structures associated with the Aquifex 16S and 23S rRNA precursors are cleaved at sites that are consistent with production of the immediate precursors to the mature rRNAs. Substrate reactivity is independent of the distal box sequence, but is strongly dependent on the proximal box sequence. RNase III mechanism of dsRNA cleavage, overview
no activation by Ca2+. The enzyme requires a divalent metal ion for catalysis, catalysis appears to be largely driven by the two metals. The adjacency of the two metal ions and their interaction with the scissile phosphodiester linkage fit the well-studied two-metal-ion catalytic mechanism, wherein one metal binds and activates the water nucleophile, and the second metal facilitates departure of the 3'-oxygen atom. Both metal ions are jointly coordinated to the side chain of a highly conserved, functionally essential glutamic acid E110
ribonuclease III cleaves double-stranded structures in bacterial RNAs and participates in diverse RNA maturation and decay pathways, RNase III mechanism of dsRNA cleavage, overview
the enzyme belongs to the ribonuclease III (RNase III) family of divalent-metal-ion-dependent phosphodiesterases. RNase III family members share a unique fold (RNase III domain) that can dimerize to form a structure that binds dsRNA and cleaves phosphodiesters on each strand, providing the characteristic 2 nt, 3'-overhang product ends. Domain structures of ribonuclease III family polypeptides, overview
crystallographic and modeling studies of RNase III from Aquifex aeolicus suggest that highly conserved six negatively charged residues, including E40/D44/D107/E110 and E37/E64, create two potential RNA cleavage sites within the catalytic valley
hanging-drop vapour-diffusion method at 19°C. Crystallisation of the mutant enzyme E110Q in complex with dsRNA 2-2 formed by self-complementary sequence 5'-CGAACUUCGCG-3', complex of wild-type enzyme with dsRNA 3-3 formed by self-complementary sequence 5'-AAAUAUAUAUUU-3', complex of wild-type enzyme with dsRNA 4-4 formed by self-complementary sequence 5'-CGCGAAUUCGCG-3' and complex of mutant enzyme E110Q with dsRNA 4-4 formed by self-complementary sequence 5'-CGCGAAUUCGCG-3'
is a conserved glutamine in the Aa-RNase III dsRNA-binding domain. Aa-RNase III cleavage of the pre-16S substrate is blocked by the Q157A mutation, which reflects a loss of substrate binding affinity. But the Q157A mutation does not affect folding or structure in a significant manner
New approaches to understanding double-stranded RNA processing by ribonuclease III purification and assays of homodimeric and heterodimeric forms of RNase III from bacterial extremophiles and mesophiles