Ribonuclease III
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RNase III
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Ribonuclease III (RNase III or RNase C)
Types of RNase III
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 a E. coli. Typically, class I enzymes possess a single RNase III domain (RIIID) followed by a dsRNA-binding domain (dsRBD).[6] They process precursors to ribosomal RNA (rRNA), small nuclear RNA (snRNA) and small 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 (UniProtKB P0A7Y0) - 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 by ribosomal protein presence.[9]
- Rnc (UniProtKB P0A7Y0) -
Class 2 RNase III
- 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]
Class 3 RNase III
- Class 3 RNases III include the Drosha family of enzymes known to function in maturation of precursors to microRNA (miRNA).[14]
Class 4 RNase III
- Class 4 RNases III include the Dicer family of enzymes known to function in RNA 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]
Human proteins containing RNase III domain
See also
References
- PMID 10713462.
- PMID 11885596.
- PMID 11809414.
- PMID 8589060.
- PMID 26438818.
- ^ a b c Liang 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
- PMID 15890961.
- ^ "rnc - Ribonuclease 3 - Escherichia coli (strain K12) - rnc gene & protein". www.uniprot.org. UniProt Consortium. Retrieved 5 November 2016.
- PMID 25634891.
- PMID 26778206.
- ^ "RNT1/YMR239C Overview". www.yeastgenome.org. Stanford University. Retrieved 5 November 2016.
- ^ "pac1 (SPBC119.11c)". www.pombase.org. EMBL-EBI. Retrieved 5 November 2016.
- PMID 10713462.
- S2CID 4371481.
- PMID 26025538.
- ^ PMID 17194582.
- PMID 18363798.
- PMID 24124076.
- ^ "Tissue expression of DICER1 - Summary". www.proteinatlas.org. The Human Protein Atlas. Retrieved 5 November 2016.
- ^ "Tissue expression of DROSHA - Summary". www.proteinatlas.org. The Human Protein Atlas. Retrieved 5 November 2016.
External links
- RNase+III at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.1.26.3