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Review for Ribonuclease III

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

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)[reply]


Ribonuclease III domain
SCOP2
1jfz / 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)

RNA Silencing, and the pnp autoregulatory mechanism [5]
.


Types of RNase III

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

File:Ribonuclease III.png
Ribonuclease III Class 1 Dimer Domain interaction with dsRNA


  • 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
    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]
.


Pac1 (UniProtKB P22192) -
S. pombe - this RNase III is located on chromosome II of the yeast nuclease and when over expressed, is directly involved in the sterility, lack of mating efficiency, abnormal mitotic cell cycle, and mutation suppression of the organism.[9]
.


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[10]
.


Class 2 RNase III



Class 3 RNase III



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

DICER1[14]


See also


External links


References

  1. ^ Cite error: The named reference undefined was invoked but never defined (see the help page).
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  3. doi:10.1016/S1097-2765(01)00418-X. {{cite journal}}: |access-date= requires |url= (help
    )
  4. doi:10.1016/S1357-2725(01)00112-1. {{cite journal}}: |access-date= requires |url= (help
    )
  5. doi:10.1016/0300-9084(96)88139-9. {{cite journal}}: |access-date= requires |url= (help
    )
  6. . Retrieved 5 November 2016.
  7. doi:10.1016/j.gene.2015.12.068. {{cite journal}}: |access-date= requires |url= (help
    )
  8. ^ "RNT1/YMR239C Overview". www.yeastgenome.org. Stanford University. Retrieved 5 November 2016.
  9. ^ "pac1 (SPBC119.11c)". www.pombase.org. EMBL-EBI. Retrieved 5 November 2016.
  10. ^ "rnc - Ribonuclease 3 - Escherichia coli (strain K12) - rnc gene & protein". www.uniprot.org. UniProt Consortium. Retrieved 5 November 2016.
  11. PMID 10713462
    .
  12. .
  13. .
  14. ^ "Tissue expression of DICER1 - Summary". www.proteinatlas.org. The Human Protein Atlas. Retrieved 5 November 2016.
  15. ^ "Tissue expression of DROSHA - Summary". www.proteinatlas.org. The Human Protein Atlas. Retrieved 5 November 2016.
This article incorporates text from the public domain Pfam and InterPro: IPR000999

Burgjane15 (talk) 21:34, 5 November 2016 (UTC)[reply]

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