Burgjane15
Review for Ribonuclease III edit
With less than two paragraphs of information in total, the article gives a one sentence definition of the function of Ribonuclease III. The sentence discusses only the generalized function of a ribonuclease and does not go into depth as to what differs it from the other classes of ribonucleases. The listing of the various classes of ribonuclease III does not provide a explanation of its importance in the various organisms it is present in or the reasons as to why it is singular in certain organisms and not others. There is a major lack in information regarding history, structure, function, history, properties, and most importantly, references. In editing this article I want to include more pictures as to its structure and reaction with cellular contents as well as a more in depth history and function description. Using sources from PubMed, NCBI, ScienceDirect, and BioMed Central, the end goal is to create a more rounded understanding as to why riboneuclease III is different than the other types of ribonucleases.
Sources for Ribonuclease III Assignment edit
Leland, P. A., & Raines, R. T. (2001). Cancer chemotherapy — ribonucleases to the rescue. Chemistry & Biology, 8(5), 405–413.
Chang-Xian Wu, Xian-Jin Xu, Ke Zheng, Fang Liu, Xu-Dong Yang, Chuang-Fu Chen, Huan-Chun Chen, Zheng-Fei Liu, Characterization of ribonuclease III from Brucella, Gene, Volume 579, Issue 2, 1 April 2016, Pages 183-192, ISSN 0378-1119, http://dx.doi.org/10.1016/j.gene.2015.12.068.[1]
Conrad, C., & Rauhut, R. (2002). Ribonuclease III: new sense from nuisance. The International Journal of Biochemistry & Cell Biology, 34(2), 116–129. https://doi.org/10.1016/S1357-2725(01)00112-1
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. https://doi.org/10.1016/0300-9084(96)88139-9
Park, H., Yakhnin, H., Connolly, M., Romeo, T., & Babitzke, P. (2015). CsrA Participates in a PNPase Autoregulatory Mechanism by Selectively Repressing Translation of pnp Transcripts That Have Been Previously Processed by RNase III and PNPase. Journal of Bacteriology, 197(24), 3751–3759. https://doi.org/10.1128/JB.00721-15
Zhang, Y., Calin-Jageman, I., Gurnon, J. R., Choi, T.-J., Adams, B., Nicholson, A. W., & Van Etten, J. L. (2003). Characterization of a chlorella virus PBCV-1 encoded ribonuclease III. Virology, 317(1), 73–83. https://doi.org/10.1016/j.virol.2003.08.044. (n.d.).
Burgjane15 (talk) 16:17, 25 October 2016 (UTC)
| Ribonuclease III domain | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Ribonuclease III structure interacting with double stranded RNA. | |||||||||||
| Identifiers | |||||||||||
| Symbol | RNase_III | ||||||||||
| Pfam | PF00636 | ||||||||||
| InterPro | IPR000999 | ||||||||||
| PROSITE | PDOC00448 | ||||||||||
| SCOP2 | 1jfz / SCOPe / SUPFAM | ||||||||||
| |||||||||||
Ribonuclease III (RNase III or RNase C)[2](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 [3]. These enzymes are a group of endoribonucleases that are characterized by their ribonuclease domain, which is labelled the RNase III domain [4]. 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 [5].
Types of RNase III edit
Within the RNase III superfamily, there are four known classes: 1, 2, 3, and 4. Each class is defined by both its functional and structural differences.
Class 1 RNase III
- Class 1 RNase III have a dimer structure whose function is to cleave dsRNA into multiple subunits. It is a Mg2+ dependent endonuclease and is largely found in bacteria, bacteriophage, and some fungi. Among the RNases III in the class are the rnc from E. coli, Pac1p from S. pombe, and Rnt1p from S. cerevisiae. They process precursors to ribosomal RNA, and in the case of fungi, process precursors to small nuclear RNA (snRNA) and small nucleolar RNA (snoRNA). The basic dsRNA cleavage function of Class 1 RNase III is similar in most of the organisms in which it is present. However, as the enzyme was conserved in various species over time, the restraints of its function has changed and expanded to meet the biological needs of each organism[6].
- Yeast nucleases with with the Class 1 RNase III domain [7]:
- RNT1 (UniProtKB Q02555) - 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[8].
Class 2 RNase III
- Class 2 RNases III include the Drosha family of enzymes known to function in maturation of precursors to miRNA.[11]
Class 3 RNase III
- Class 3 RNases III include the Dicer family of enzymes known to function in RNA interference (RNAi).[12]
Class 4 RNase III
- Class 4 RNases III, called Mini-III, are homodimeric enzymes and consist solely of the RNase III domains.[13]
Human proteins containing RNase III domain edit
See also edit
External links edit
- RNase+III at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.1.26.3
References edit
- ^ Cite error: The named reference
undefinedwas invoked but never defined (see the help page). - ^ 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.
- ^ Zamore, Phollip 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.
{{cite journal}}:|access-date=requires|url=(help) - ^ 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.
{{cite journal}}:|access-date=requires|url=(help) - ^ 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.
{{cite journal}}:|access-date=requires|url=(help) - ^ Kreuze, Jan F.; Savenkov, Eugene I.; Cuellar, Wilmer; Li, Xiangdong; Valkonen, Jari P. T. (1 June 2005). "Viral Class 1 RNase III Involved in Suppression of RNA Silencing". Journal of Virology. 79 (11): 7227–7238. doi:10.1128/JVI.79.11.7227-7238.2005. ISSN 0022-538X. Retrieved 5 November 2016.
- ^ Wu, Chang-Xian; Xu, Xian-Jin; Zheng, Ke; Liu, Fang; Yang, Xu-Dong; Chen, Chuang-Fu; Chen, Huan-Chun; Liu, Zheng-Fei (1 April 2016). "Characterization of ribonuclease III from Brucella". Gene. 579 (2): 183–192. doi:10.1016/j.gene.2015.12.068.
{{cite journal}}:|access-date=requires|url=(help) - ^ "RNT1/YMR239C Overview". www.yeastgenome.org. Stanford University. Retrieved 5 November 2016.
- ^ "pac1 (SPBC119.11c)". www.pombase.org. EMBL-EBI. Retrieved 5 November 2016.
- ^ "rnc - Ribonuclease 3 - Escherichia coli (strain K12) - rnc gene & protein". www.uniprot.org. UniProt Consortium. Retrieved 5 November 2016.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ "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.
Burgjane15 (talk) 21:34, 5 November 2016 (UTC)
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