Ribonuclease III (RNase III or RNase C)[1](BRENDA3.1.26.3) is a type ofribonuclease that recognizesdsRNA and cleaves it at specific targeted locations to transform them into mature RNAs.[2] These enzymes are a group ofendoribonucleases 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 asRNA precursor synthesis,RNA Silencing, and thepnp autoregulatory mechanism.[4][5]
The RNase III superfamily is divided into four known classes: 1, 2, 3, and 4. Each class is defined by its domain structure.[6]
Class 1 RNase III
Class 1 RNase III enzymes have ahomodimeric structure whose function is to cleave dsRNA into multiple subunits. It is a Mg2+-dependent endonuclease and is largely found inbacteria andbacteriophage. Class 1 RNase III have been found in Glomeromycotanfungi, which was suspected to be the result ofhorizontal gene transfer fromcyanobacteria.[7] Among the RNases III in the class are the rnc fromE. coli. Typically, class I enzymes possess a single RNase III domain (RIIID) followed by a dsRNA-binding domain (dsRBD).[6] They process precursors toribosomal RNA (rRNA),small nuclear RNA (snRNA) andsmall nucleolar RNA (snoRNA). The basic dsRNA cleavage function of Class 1 RNase III is retained in most of the organisms in which it is present. However, in a number of species the function has changed and taken on different or additional biological roles.[8]
Rnc (UniProtKBP0A7Y0) -E.Coli - this RNase III is involved in the processing of viral transcripts and some mRNAs through the cleavage of multiple areas on the dsRNA. This cleavage can be influenced byribosomal protein presence.[9]
The variances of Class 1 RNase III, calledMini-III, are homodimeric enzymes and consist solely of the RNase III domains.[10]
Class 2 RNase III
Class 2 ribonuclease III (Rnt1p) from Saccharomyces cerevisiae in complex with double-stranded RNA
Class II is defined by the presence of an N-terminal domain (NTD), a RIIID, and a dsRBD. Class II is found in some fungi species.[6] They process precursors to rRNA, snRNA, and snoRNA.
Yeast nucleases with the Class 2 RNase III domain:[11]
RNT1 (UniProtKBQ02555) -S. cerevisiae - this RNase III is involved in the transcription and processing of rDNA, the 3' end formation of U2 snRNA via cleavage of the terminal loop, cell wall stress response and degradation, and regulation of morphogenesis checkpoint genes.[12]
Pac1 (UniProtKBP22192) -S. pombe - this RNase III is located on chromosome II of the yeast genome and, when over expressed, is directly involved in the sterility, lack of mating efficiency, abnormal mitotic cell cycle, and mutation suppression of the organism.[13]
Class 3 RNase III
The crystal structure of the human Drosha ribonuclease enzyme in complex with two C-terminal helices of the DGCR8 protein.
Class 3 RNases III include theDrosha family of enzymes known to function in maturation of precursors tomicroRNA (miRNA).[14]
Class 4 RNase III
Class 4 RNases III include theDicer family of enzymes known to function inRNA interference (RNAi).[15] Class 4 III RNases are S-RNase components. It is a component of the self-incompatibility system in Rosaceae, Solanaceae, and Plantaginaceae. They are recruited to cope with various environmental stress scenarios.[16]
Dicer enzymes process dsRNA substrates into small RNA fragments of individual size ranging from 21-27 nucleotides in length.[17] Dicer has an N-terminal helicase/ATPase domain which is followed by another domain of an unknown function. It also comprises the centrally positioned PAZ domain and a C-terminal configuration which includes one dsRBD and two RNase III catalytic domains.[18] Interactions of Dicer occurs with other proteins, which includes TRBP, PACT, and Ago2.[19] RNAs that are produced by Dicer act as guides for a sequence of particular silencing of cognate genes through RNAi and related pathways.[17]
^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.PMID10713462.
^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.PMID11809414.
^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.PMID8589060.
^abcLiang Y-H, Lavoie M, Comeau M-A, Elela SA, Ji X. Structure of a Eukaryotic RNase III Post-Cleavage Complex Reveals a Double- Ruler Mechanism for Substrate Selection. Molecular cell. 2014;54(3):431-444. doi:10.1016/j.molcel.2014.03.006.
^Soon-Jae Lee, Mengxuan Kong, Paul Harrison, Mohamed Hijri; Conserved proteins of the RNA interference system in the arbuscular mycorrhizal fungus Rhizoglomus irregulare provide new insight into the evolutionary history of Glomeromycota, Genome Biology and Evolution, evy002,https://doi.org/10.1093/gbe/evy002
^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.PMID10713462.
^abMacRae, Ian J; Doudna, Jennifer A (February 2007). "Ribonuclease revisited: structural insights into ribonuclease III family enzymes".Current Opinion in Structural Biology.17 (1):138–145.doi:10.1016/j.sbi.2006.12.002.PMID17194582.
