Ribonuclease III

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Ribonuclease III domain
PDB 1yyw EBI.jpg
Ribonuclease III structure interacting with double stranded RNA.
Symbol RNase_III
Pfam PF00636
InterPro IPR000999
SCOP 1jfz

RNase III enzymes specifically bind to and cleave double-stranded RNA (dsRNA).[1] There are four subdivisions, known as Class 1, 2, 3, and 4.

Prokaryotic ribonuclease III (EC (gene rnc)[2] is an enzyme that digests double-stranded RNA. It is involved in the processing of ribosomal RNA precursors and of some mRNAs.

  • Class 2 RNases III include the Drosha family of enzymes known to function in maturation of precursors to miRNA.[3]
  • Class 4 RNases III called Mini-III are homodimeric enzymes and consist solely of the RNase III domains.[5]

Human proteins containing this domain[edit]


See also[edit]

External links[edit]


  1. ^ Lamontagne, B.; Larose, S.; Boulanger, J.; Elela, S. (2001). "The RNase III family: A conserved structure and expanding functions in eukaryotic dsRNA metabolism". Current issues in molecular biology 3 (4): 71–78. PMID 11719970. 
  2. ^ Nashimoto H, Uchida H (1985). "DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations". Mol. Gen. Genet. 201 (1): 25–29. doi:10.1007/bf00397981. PMID 3903434. 
  3. ^ Filippov V, Solovyev V, Filippova M, Gill SS (Mar 2000). "A novel type of RNase III family proteins in eukaryotes". Gene 245 (1): 213–221. doi:10.1016/S0378-1119(99)00571-5. PMID 10713462. 
  4. ^ Bernstein E, Caudy AA, Hammond SM, Hannon GJ (2001). "Role for a bidentate ribonuclease in the initiation step of RNA interference". Nature 409 (6818): 363–6. doi:10.1038/35053110. PMID 11201747. 
  5. ^ Glow, D.; Pianka, D.; Sulej, A. A.; Kozlowski, Lukasz P.; Czarnecka, J.; Chojnowski, G.; Skowronek, K. J.; Bujnicki, J. M. (2015). "Sequence-specific cleavage of dsRNA by Mini-III RNase". Nucleic Acids Research 43 (5): 2864–2873. doi:10.1093/nar/gkv009. ISSN 0305-1048. PMID 25634891. 

This article incorporates text from the public domain Pfam and InterPro IPR000999