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Literature summary extracted from
- Ribonuclease III mechanisms of double-stranded RNA cleavage (2013), Wiley Interdiscip. Rev. RNA, 5, 31-48.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.26.3 | additional information | T7-induced catalytic enhancement of the enzyme | Escherichia coli |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.26.3 | crystal structure analysis of wild-type enzyme and D44N mutant enzyme | Aquifex aeolicus |
| 3.1.26.3 | crystal structure analysis, PDB ID 1O0W | Thermotoga maritima |
| 3.1.26.3 | crystal structure analysis, PDB ID 2A11 | Mycobacterium tuberculosis |
| 3.1.26.3 | crystal structure analysis, PDB ID 2ffl, crystallographic analysis of the minimal Dicer of Giardia intestinalis, containing the PAZ and tandem RNase III domainsl | Giardia intestinalis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | D44N | site-directed mutagenesis, the mutation does not fully inactivate the enzyme, and dsRNA cleavage occurs during crystallization of the mutant enzyme | Aquifex aeolicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.26.3 | additional information | the RNase III activity in vivo is responsive to osmotic stress | Escherichia coli |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.26.3 | cytoplasm | dicer | Homo sapiens | 5737 | - |
| 3.1.26.3 | nucleus | drosha | Homo sapiens | 5634 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.26.3 | Co2+ | activates | Escherichia coli |  |
| 3.1.26.3 | Co2+ | activates | Homo sapiens | |
| 3.1.26.3 | Co2+ | activates | Saccharomyces cerevisiae | |
| 3.1.26.3 | Co2+ | activates | Schizosaccharomyces pombe | |
| 3.1.26.3 | Co2+ | activates | Aquifex aeolicus | |
| 3.1.26.3 | Co2+ | activates | Thermotoga maritima | |
| 3.1.26.3 | Co2+ | activates | Mycobacterium tuberculosis | |
| 3.1.26.3 | Co2+ | activates | Giardia intestinalis | |
| 3.1.26.3 | Mg2+ | activates | Escherichia coli | |
| 3.1.26.3 | Mg2+ | activates | Homo sapiens | |
| 3.1.26.3 | Mg2+ | activates | Saccharomyces cerevisiae | |
| 3.1.26.3 | Mg2+ | activates | Schizosaccharomyces pombe | |
| 3.1.26.3 | Mg2+ | activates | Aquifex aeolicus | |
| 3.1.26.3 | Mg2+ | activates | Thermotoga maritima | |
| 3.1.26.3 | Mg2+ | activates | Mycobacterium tuberculosis | |
| 3.1.26.3 | Mg2+ | activates | Giardia intestinalis | |
| 3.1.26.3 | Mn2+ | activates | Escherichia coli | |
| 3.1.26.3 | Mn2+ | activates | Homo sapiens | |
| 3.1.26.3 | Mn2+ | activates | Saccharomyces cerevisiae | |
| 3.1.26.3 | Mn2+ | activates | Schizosaccharomyces pombe | |
| 3.1.26.3 | Mn2+ | activates | Aquifex aeolicus | |
| 3.1.26.3 | Mn2+ | activates | Thermotoga maritima | |
| 3.1.26.3 | Mn2+ | activates | Mycobacterium tuberculosis | |
| 3.1.26.3 | Mn2+ | activates | Giardia intestinalis | |
| 3.1.26.3 | additional information | 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 | Aquifex aeolicus | |
| 3.1.26.3 | additional information | 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 E117 | Escherichia coli | |
| 3.1.26.3 | additional information | the enzyme requires a divalent metal ion for catalysis | Homo sapiens | |
| 3.1.26.3 | additional information | the enzyme requires a divalent metal ion for catalysis | Saccharomyces cerevisiae | |
| 3.1.26.3 | additional information | the enzyme requires a divalent metal ion for catalysis | Schizosaccharomyces pombe | |
| 3.1.26.3 | additional information | the enzyme requires a divalent metal ion for catalysis | Thermotoga maritima | |
| 3.1.26.3 | additional information | the enzyme requires a divalent metal ion for catalysis | Mycobacterium tuberculosis | |
| 3.1.26.3 | additional information | the enzyme requires a divalent metal ion for catalysis | Giardia intestinalis | |
| 3.1.26.3 | Ni2+ | activates | Escherichia coli | |
| 3.1.26.3 | Ni2+ | activates | Homo sapiens | |
| 3.1.26.3 | Ni2+ | activates | Saccharomyces cerevisiae | |
| 3.1.26.3 | Ni2+ | activates | Schizosaccharomyces pombe | |
| 3.1.26.3 | Ni2+ | activates | Aquifex aeolicus | |
| 3.1.26.3 | Ni2+ | activates | Thermotoga maritima | |
| 3.1.26.3 | Ni2+ | activates | Mycobacterium tuberculosis | |
| 3.1.26.3 | Ni2+ | activates | Giardia intestinalis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.3 | additional information | Aquifex aeolicus | processing of dsRNA | ? | - |
? | |
| 3.1.26.3 | additional information | Thermotoga maritima | processing of dsRNA | ? | - |
? | |
| 3.1.26.3 | additional information | Mycobacterium tuberculosis | processing of dsRNA | ? | - |
? | |
| 3.1.26.3 | additional information | Saccharomyces cerevisiae | processing of dsRNA, specific bp sequence elements can modulate substrate reactivity, and a network of hydrogen bonds provides an energetically important contribution to Rnt1p binding, a phylogenetic-based substrate alignment analysis reveals a statistically significant exclusion of the UA bp from the position adjacent to the tetraloop. Rnt1p cleaves hairpin structures in pre-rRNAs, pre-mRNAs, and transcripts containing noncoding RNAs such as snoRNAs, as part of the respective maturation pathways. The enzyme also interacts with Gar1p, a protein involved in pseudouridylation reactions, via its C-terminal portion adjacent to the dsRBD | ? | - |
? | |
| 3.1.26.3 | additional information | Giardia intestinalis | processing of dsRNA, the PAZ domain specifically recognizes the 2-nt, 3'-overhangs of a processed dsRNA terminus | ? | - |
? | |
| 3.1.26.3 | additional information | Homo sapiens | processing of dsRNA. Drosha acts on primary transcripts synthesized by RNA polymerase II that typically contain several miRNAs. Site-specific cleavage within irregular, extended hairpin structures (pri-miRNAs) creates the pre-miRNAs that then are delivered by Exportin5 to the cytoplasm for final maturation by Dicer. Drosha functions within a complex termed the microprocessor that contains a protein, DGCR8, that is required for Drosha action | ? | - |
? | |
| 3.1.26.3 | additional information | Schizosaccharomyces pombe | processing of dsRNA. Pac1p cleaves hairpin structures in pre-rRNAs, pre-mRNAs, and transcripts containing noncoding RNAs such as snoRNAs, as part of the respective maturation pathways | ? | - |
? | |
| 3.1.26.3 | additional information | Escherichia coli | the enzyme cleaves the proU operon transcript reducing its half-life from 65 sec to 4 sec, the rapid degradation ensures efficient inhibition of proU expression and further uptake of osmoprotectants. Processing of dsRNA, product release is the rate-limiting step in the catalytic pathway | ? | - |
? | |
| 3.1.26.3 | additional information | Mycobacterium tuberculosis H37Rv | processing of dsRNA | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.3 | Aquifex aeolicus | O67082 | - |
- |
| 3.1.26.3 | Escherichia coli | - |
- |
- |
| 3.1.26.3 | Giardia intestinalis | A8BQJ3 | - |
- |
| 3.1.26.3 | Homo sapiens | - |
- |
- |
| 3.1.26.3 | Mycobacterium tuberculosis | P9WH03 | - |
- |
| 3.1.26.3 | Mycobacterium tuberculosis H37Rv | P9WH03 | - |
- |
| 3.1.26.3 | Saccharomyces cerevisiae | - |
- |
- |
| 3.1.26.3 | Schizosaccharomyces pombe | - |
- |
- |
| 3.1.26.3 | Thermotoga maritima | Q9X0I6 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | phosphoprotein | phosphorylation on a serine in the RNase III domain activates the enzyme, the covalent modification facilitates product release, which is the rate-limiting step in the catalytic pathway | Escherichia coli |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.1.26.3 | 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 | Homo sapiens | |
| 3.1.26.3 | 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 | Saccharomyces cerevisiae | |
| 3.1.26.3 | 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 | Schizosaccharomyces pombe | |
| 3.1.26.3 | 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 | Aquifex aeolicus | |
| 3.1.26.3 | 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 | Thermotoga maritima | |
| 3.1.26.3 | 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 | Mycobacterium tuberculosis | |
| 3.1.26.3 | 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 | Giardia intestinalis | |
| 3.1.26.3 | 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, essential irreversibility of the hydrolytic step | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.3 | additional information | processing of dsRNA | Aquifex aeolicus | ? | - |
? | |
| 3.1.26.3 | additional information | processing of dsRNA | Thermotoga maritima | ? | - |
? | |
| 3.1.26.3 | additional information | processing of dsRNA | Mycobacterium tuberculosis | ? | - |
? | |
| 3.1.26.3 | additional information | processing of dsRNA, specific bp sequence elements can modulate substrate reactivity, and a network of hydrogen bonds provides an energetically important contribution to Rnt1p binding, a phylogenetic-based substrate alignment analysis reveals a statistically significant exclusion of the UA bp from the position adjacent to the tetraloop. Rnt1p cleaves hairpin structures in pre-rRNAs, pre-mRNAs, and transcripts containing noncoding RNAs such as snoRNAs, as part of the respective maturation pathways. The enzyme also interacts with Gar1p, a protein involved in pseudouridylation reactions, via its C-terminal portion adjacent to the dsRBD | Saccharomyces cerevisiae | ? | - |
? | |
| 3.1.26.3 | additional information | processing of dsRNA, the PAZ domain specifically recognizes the 2-nt, 3'-overhangs of a processed dsRNA terminus | Giardia intestinalis | ? | - |
? | |
| 3.1.26.3 | additional information | processing of dsRNA. Drosha acts on primary transcripts synthesized by RNA polymerase II that typically contain several miRNAs. Site-specific cleavage within irregular, extended hairpin structures (pri-miRNAs) creates the pre-miRNAs that then are delivered by Exportin5 to the cytoplasm for final maturation by Dicer. Drosha functions within a complex termed the microprocessor that contains a protein, DGCR8, that is required for Drosha action | Homo sapiens | ? | - |
? | |
| 3.1.26.3 | additional information | processing of dsRNA. Pac1p cleaves hairpin structures in pre-rRNAs, pre-mRNAs, and transcripts containing noncoding RNAs such as snoRNAs, as part of the respective maturation pathways | Schizosaccharomyces pombe | ? | - |
? | |
| 3.1.26.3 | additional information | the enzyme cleaves the proU operon transcript reducing its half-life from 65 sec to 4 sec, the rapid degradation ensures efficient inhibition of proU expression and further uptake of osmoprotectants. Processing of dsRNA, product release is the rate-limiting step in the catalytic pathway | Escherichia coli | ? | - |
? | |
| 3.1.26.3 | additional information | Dicer substrate recognition and specificity, overview | Giardia intestinalis | ? | - |
? | |
| 3.1.26.3 | additional information | Drosha cleavage site analysis, reactivity determinants of a pri-miRNA substrate for Drosha, and a proposed DGCR8-dsRNA interaction, and Dicer substrate recognition and specificity, overview | Homo sapiens | ? | - |
? | |
| 3.1.26.3 | additional information | processing of dsRNA | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | homodimer | - |
Escherichia coli |
| 3.1.26.3 | homodimer | - |
Saccharomyces cerevisiae |
| 3.1.26.3 | homodimer | - |
Schizosaccharomyces pombe |
| 3.1.26.3 | homodimer | - |
Aquifex aeolicus |
| 3.1.26.3 | homodimer | - |
Thermotoga maritima |
| 3.1.26.3 | homodimer | - |
Mycobacterium tuberculosis |
| 3.1.26.3 | homodimer | the Drosha polypeptide possesses tandem RNase III domains and a C-terminal dsRBD. The RNase III domains form an intramolecular pseudodimer with two catalytic sites. The Drosha dsRBD structure shows an alpha1-alpha1 loop element with a dynamic, extended structure | Homo sapiens |
| 3.1.26.3 | homodimer | the minimal Dicer of Giardia intestinalis contains the PAZ and tandem RNase III domains, pseudodimeric RNase III domain | Giardia intestinalis |
| 3.1.26.3 | More | inability of the Drosha dsRBD to form a stable complex on its own with dsRNA. Dicer structure analysis, overview | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | Dicer | - |
Homo sapiens |
| 3.1.26.3 | Dicer | - |
Giardia intestinalis |
| 3.1.26.3 | Drosha | - |
Homo sapiens |
| 3.1.26.3 | Pac1p | - |
Schizosaccharomyces pombe |
| 3.1.26.3 | RNase III | - |
Escherichia coli |
| 3.1.26.3 | RNase III | - |
Homo sapiens |
| 3.1.26.3 | RNase III | - |
Saccharomyces cerevisiae |
| 3.1.26.3 | RNase III | - |
Schizosaccharomyces pombe |
| 3.1.26.3 | RNase III | - |
Aquifex aeolicus |
| 3.1.26.3 | RNase III | - |
Thermotoga maritima |
| 3.1.26.3 | RNase III | - |
Mycobacterium tuberculosis |
| 3.1.26.3 | RNase III | - |
Giardia intestinalis |
| 3.1.26.3 | Rnt1p | - |
Saccharomyces cerevisiae |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.26.3 | evolution | 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 | Escherichia coli |
| 3.1.26.3 | evolution | 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 | Saccharomyces cerevisiae |
| 3.1.26.3 | evolution | 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 | Schizosaccharomyces pombe |
| 3.1.26.3 | evolution | 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 | Aquifex aeolicus |
| 3.1.26.3 | evolution | 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 | Thermotoga maritima |
| 3.1.26.3 | evolution | 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 | Mycobacterium tuberculosis |
| 3.1.26.3 | evolution | 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 | Giardia intestinalis |
| 3.1.26.3 | evolution | the enzyme belongs to the 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 | Homo sapiens |
| 3.1.26.3 | additional information | features of the Rnt1p-substrate interaction contributing to processing reactivity, overview. Structure analysis and comparison to other enzyme family members, overview | Saccharomyces cerevisiae |
| 3.1.26.3 | additional information | structure analysis and comparison to other enzyme family members, overview | Escherichia coli |
| 3.1.26.3 | additional information | structure analysis and comparison to other enzyme family members, overview | Schizosaccharomyces pombe |
| 3.1.26.3 | additional information | structure analysis and comparison to other enzyme family members, overview | Aquifex aeolicus |
| 3.1.26.3 | additional information | structure analysis and comparison to other enzyme family members, overview | Thermotoga maritima |
| 3.1.26.3 | additional information | structure analysis and comparison to other enzyme family members, overview | Mycobacterium tuberculosis |
| 3.1.26.3 | additional information | structure analysis and comparison to other enzyme family members, overview. Additional domains, including the dsRNA-binding and PAZ domains, that cooperate with the RNase III domain to select target sites, regulate activity, confer processivity, and support the recognition of structurally diverse substrates | Homo sapiens |
| 3.1.26.3 | additional information | structure analysis and comparison to other enzyme family members, overview. Additional domains, including the dsRNA-binding and PAZ domains, that cooperate with the RNase III domain to select target sites, regulate activity, confer processivity, and support the recognition of structurally diverse substrates | Giardia intestinalis |
| 3.1.26.3 | physiological function | processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs | Homo sapiens |
| 3.1.26.3 | physiological function | processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs | Aquifex aeolicus |
| 3.1.26.3 | physiological function | processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs | Thermotoga maritima |
| 3.1.26.3 | physiological function | processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs | Mycobacterium tuberculosis |
| 3.1.26.3 | physiological function | processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs | Giardia intestinalis |
| 3.1.26.3 | physiological function | processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs. RNase III is negatively regulated by the macrodomain protein, YmdB, and might be dependent upon the direct interaction of the two proteins. The enzyme's catalytic activity is also subject to positive regulation. The T7 bacteriophage expresses a protein kinase that phosphorylates RNase III and enhances catalytic activity about fourfold, as measured in vitro | Escherichia coli |
| 3.1.26.3 | physiological function | the enzyme is involved in RNA quality control. Processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs | Saccharomyces cerevisiae |
| 3.1.26.3 | physiological function | the enzyme is involved in RNA quality control. Processing of dsRNA by the enzyme is an essential step in the maturation and decay of coding and noncoding RNAs, including miRNAs and siRNAs | Schizosaccharomyces pombe |
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