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Literature summary for 3.1.26.3 extracted from

  • Ji, X.
    Structural basis for non-catalytic and catalytic activities of ribonuclease III (2006), Acta Crystallogr. Sect. D, 62, 933-940.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
12 three-dimensional structures of bacterial RNase III in various forms have been reported Escherichia coli
12 three-dimensional structures of bacterial RNase III in various forms have been reported Aquifex aeolicus
in complex with dsRNA, in the presence of Mg2+ or Mn2+ one metal ion bound per polypeptide chain Aquifex aeolicus
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

Protein Variants Comment Organism
D44N mutation of the cleavage site Aquifex aeolicus
E110A uncoupling of the dsRNA-binding and processing abilities of the enzyme Aquifex aeolicus
E110K loss of Mg2+ binding capacity, non-functional, uncoupling of the dsRNA-binding and processing abilities of the enzyme Aquifex aeolicus
E110K mutation of the cleavage site Aquifex aeolicus
E110Q uncoupling of the dsRNA-binding and processing abilities of the enzyme Aquifex aeolicus
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

Metals/Ions Comment Organism Structure
Ca2+ inactive Escherichia coli
Co2+ can substitute for Mg2+ Escherichia coli
Mg2+
-
Escherichia coli
Mg2+
-
Aquifex aeolicus
Mg2+
-
Homo sapiens
Mg2+
-
Saccharomyces cerevisiae
Mg2+ required Escherichia coli
Mg2+ required Aquifex aeolicus
Mn2+
-
Aquifex aeolicus
Mn2+ can substitute for Mg2+ Escherichia coli
Ni2+ can substitute for Mg2+ Escherichia coli
Sr2+ inactive Escherichia coli
Zn2+ inactive Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
double-stranded RNA + H2O Aquifex aeolicus responsible for processing of dsRNA 5'-phosphooligonucleotides
-
?
double-stranded RNA + H2O Thermotoga maritima responsible for processing of dsRNA 5'-phosphooligonucleotides small duplex products of 10-18 base pairs ?
double-stranded RNA + H2O Escherichia coli responsible for processing of dsRNA 5'-phosphooligonucleotides small duplex products of 10-18 base pairs ?
additional information Escherichia coli as a binding protein, RNase III binds and stabilizes certain RNAs, thus suppressing the expression of certain genes ?
-
?

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus O67082
-
-
Escherichia coli P0A7Y0
-
-
Escherichia coli P0A7Y0 K12
-
Homo sapiens Q9NRR4
-
-
Homo sapiens Q9UPY3
-
-
Saccharomyces cerevisiae Q02555
-
-
Thermotoga maritima
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
double-stranded RNA + H2O responsible for processing of dsRNA Aquifex aeolicus 5'-phosphooligonucleotides
-
?
double-stranded RNA + H2O responsible for processing of dsRNA Thermotoga maritima 5'-phosphooligonucleotides small duplex products of 10-18 base pairs ?
double-stranded RNA + H2O responsible for processing of dsRNA Escherichia coli 5'-phosphooligonucleotides small duplex products of 10-18 base pairs ?
additional information as a binding protein, RNase III binds and stabilizes certain RNAs, thus suppressing the expression of certain genes Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer
-
Thermotoga maritima
dimer
-
Escherichia coli
dimer
-
Aquifex aeolicus

Synonyms

Synonyms Comment Organism
Aa-RNase III
-
Aquifex aeolicus
Dicer
-
Homo sapiens
Drosha
-
Homo sapiens
Ec-RNase III
-
Escherichia coli
Hs-Dicer
-
Homo sapiens
Hs-Drosha
-
Homo sapiens
ribonuclease III
-
Aquifex aeolicus
ribonuclease III
-
Homo sapiens
RNase III
-
Escherichia coli
RNase III
-
Aquifex aeolicus
RNase III
-
Homo sapiens
Rnt1p
-
Saccharomyces cerevisiae
Sc-Rnt1p
-
Saccharomyces cerevisiae
Tm-RNase III
-
Thermotoga maritima