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Literature summary extracted from
- Structural basis for non-catalytic and catalytic activities of ribonuclease III (2006), Acta Crystallogr. Sect. D, 62, 933-940.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.26.3 | 12 three-dimensional structures of bacterial RNase III in various forms have been reported | Escherichia coli |
| 3.1.26.3 | 12 three-dimensional structures of bacterial RNase III in various forms have been reported | Aquifex aeolicus |
| 3.1.26.3 | in complex with dsRNA, in the presence of Mg2+ or Mn2+ one metal ion bound per polypeptide chain | Aquifex aeolicus |
| 3.1.26.3 | RNA-free structure of full length RNase III, comparison with crystal structures of Aquifex aeolicus RNase-dsRNA complex indicates dramatic conformational changes upon dsRNA binding | Thermotoga maritima |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | D44N | mutation of the cleavage site | Aquifex aeolicus |
| 3.1.26.3 | E110A | uncoupling of the dsRNA-binding and processing abilities of the enzyme | Aquifex aeolicus |
| 3.1.26.3 | E110K | loss of Mg2+ binding capacity, non-functional, uncoupling of the dsRNA-binding and processing abilities of the enzyme | Aquifex aeolicus |
| 3.1.26.3 | E110K | mutation of the cleavage site | Aquifex aeolicus |
| 3.1.26.3 | E110Q | uncoupling of the dsRNA-binding and processing abilities of the enzyme | Aquifex aeolicus |
| 3.1.26.3 | Q153P | the Q153P substitution in the middle of the flexible linker between the endoND and the dsRBD abolish RNA-cleavage activity | Escherichia coli |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.26.3 | Ca2+ | inactive | Escherichia coli |  |
| 3.1.26.3 | Co2+ | can substitute for Mg2+ | Escherichia coli | |
| 3.1.26.3 | Mg2+ | - |
Escherichia coli | |
| 3.1.26.3 | Mg2+ | - |
Aquifex aeolicus | |
| 3.1.26.3 | Mg2+ | - |
Homo sapiens | |
| 3.1.26.3 | Mg2+ | - |
Saccharomyces cerevisiae | |
| 3.1.26.3 | Mg2+ | required | Escherichia coli | |
| 3.1.26.3 | Mg2+ | required | Aquifex aeolicus | |
| 3.1.26.3 | Mn2+ | - |
Aquifex aeolicus | |
| 3.1.26.3 | Mn2+ | can substitute for Mg2+ | Escherichia coli | |
| 3.1.26.3 | Ni2+ | can substitute for Mg2+ | Escherichia coli | |
| 3.1.26.3 | Sr2+ | inactive | Escherichia coli | |
| 3.1.26.3 | Zn2+ | inactive | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.3 | double-stranded RNA + H2O | Aquifex aeolicus | responsible for processing of dsRNA | 5'-phosphooligonucleotides | - |
? | |
| 3.1.26.3 | double-stranded RNA + H2O | Thermotoga maritima | responsible for processing of dsRNA | 5'-phosphooligonucleotides | small duplex products of 10-18 base pairs | ? | |
| 3.1.26.3 | double-stranded RNA + H2O | Escherichia coli | responsible for processing of dsRNA | 5'-phosphooligonucleotides | small duplex products of 10-18 base pairs | ? | |
| 3.1.26.3 | additional information | Escherichia coli | as a binding protein, RNase III binds and stabilizes certain RNAs, thus suppressing the expression of certain genes | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.3 | Aquifex aeolicus | O67082 | - |
- |
| 3.1.26.3 | Escherichia coli | P0A7Y0 | - |
- |
| 3.1.26.3 | Escherichia coli | P0A7Y0 | K12 | - |
| 3.1.26.3 | Homo sapiens | Q9NRR4 | - |
- |
| 3.1.26.3 | Homo sapiens | Q9UPY3 | - |
- |
| 3.1.26.3 | Saccharomyces cerevisiae | Q02555 | - |
- |
| 3.1.26.3 | Thermotoga maritima | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.3 | double-stranded RNA + H2O | responsible for processing of dsRNA | Aquifex aeolicus | 5'-phosphooligonucleotides | - |
? | |
| 3.1.26.3 | double-stranded RNA + H2O | responsible for processing of dsRNA | Thermotoga maritima | 5'-phosphooligonucleotides | small duplex products of 10-18 base pairs | ? | |
| 3.1.26.3 | double-stranded RNA + H2O | responsible for processing of dsRNA | Escherichia coli | 5'-phosphooligonucleotides | small duplex products of 10-18 base pairs | ? | |
| 3.1.26.3 | additional information | as a binding protein, RNase III binds and stabilizes certain RNAs, thus suppressing the expression of certain genes | Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | dimer | - |
Thermotoga maritima |
| 3.1.26.3 | dimer | - |
Escherichia coli |
| 3.1.26.3 | dimer | - |
Aquifex aeolicus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | Aa-RNase III | - |
Aquifex aeolicus |
| 3.1.26.3 | Dicer | - |
Homo sapiens |
| 3.1.26.3 | Drosha | - |
Homo sapiens |
| 3.1.26.3 | Ec-RNase III | - |
Escherichia coli |
| 3.1.26.3 | Hs-Dicer | - |
Homo sapiens |
| 3.1.26.3 | Hs-Drosha | - |
Homo sapiens |
| 3.1.26.3 | ribonuclease III | - |
Aquifex aeolicus |
| 3.1.26.3 | ribonuclease III | - |
Homo sapiens |
| 3.1.26.3 | RNase III | - |
Escherichia coli |
| 3.1.26.3 | RNase III | - |
Aquifex aeolicus |
| 3.1.26.3 | RNase III | - |
Homo sapiens |
| 3.1.26.3 | Rnt1p | - |
Saccharomyces cerevisiae |
| 3.1.26.3 | Sc-Rnt1p | - |
Saccharomyces cerevisiae |
| 3.1.26.3 | Tm-RNase III | - |
Thermotoga maritima |
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