Ribonuclease III

Ribonuclease III domain
Ribonuclease III structure interacting with double stranded RNA.
Identifiers
SymbolRNase_III
PfamPF00636
InterProIPR000999
PROSITEPDOC00448
SCOP21jfz / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1o0wB:51-141 2a11A:41-134 1jfzA:37-121

1rc7A:37-121 1yywA:37-121 1i4sA:37-121 1rc5B:37-121 1yyoA:37-121 1yykB:37-121

1yz9A:37-121 2fflA:333-418 1u61A:10-111

Ribonuclease III (RNase III or RNase C)[1](BRENDA 3.1.26.3) is a type of ribonuclease that recognizes dsRNA and cleaves it at specific targeted locations to transform them into mature RNAs.[2] These enzymes are a group of endoribonucleases that are characterized by their ribonuclease domain, which is labelled the RNase III domain.[3] They are ubiquitous compounds in the cell and play a major role in pathways such as RNA precursor synthesis, RNA Silencing, and the pnp autoregulatory mechanism.[4][5]

  1. ^ Filippov, Valery; Solovyev, Victor; Filippova, Maria; Gill, Sarjeet S. (7 March 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.
  2. ^ Zamore, Phillip D. (December 2001). "Thirty-Three Years Later, a Glimpse at the Ribonuclease III Active Site". Molecular Cell. 8 (6): 1158–1160. doi:10.1016/S1097-2765(01)00418-X. PMID 11885596.
  3. ^ Conrad, Christian; Rauhut, Reinhard (February 2002). "Ribonuclease III: new sense from nuisance". The International Journal of Biochemistry & Cell Biology. 34 (2): 116–129. doi:10.1016/S1357-2725(01)00112-1. PMID 11809414.
  4. ^ Inada, T.; Nakamura, Y. (1995). "Lethal double-stranded RNA processing activity of ribonuclease III in the absence of SuhB protein of Escherichia coli". Biochimie. 77 (4): 294–302. doi:10.1016/0300-9084(96)88139-9. PMID 8589060.
  5. ^ Park, Hongmarn; Yakhnin, Helen; Connolly, Michael; Romeo, Tony; Babitzke, Paul; Gourse, R. L. (15 December 2015). "CsrA Participates in a PNPase Autoregulatory Mechanism by Selectively Repressing Translation of Transcripts That Have Been Previously Processed by RNase III and PNPase". Journal of Bacteriology. 197 (24): 3751–3759. doi:10.1128/JB.00721-15. PMC 4652041. PMID 26438818.