User:ExasperatedOctopus/sandbox: Difference between revisions
added some clarification |
Added why we care about decapping mRNA |
||
| Line 1: | Line 1: | ||
Sources for the article [[Decapping complex|Decapping Complex]]: This is a review<ref name=":0">{{Cite journal|last=Charenton|first=Clément|last2=Graille|first2=Marc|date=2018-12-19|title=mRNA decapping: finding the right structures|url=https://royalsocietypublishing.org/doi/10.1098/rstb.2018.0164|journal=Philosophical Transactions of the Royal Society B: Biological Sciences|volume=373|issue=1762|pages=20180164|doi=10.1098/rstb.2018.0164|pmc=PMC6232594|pmid=30397101}}</ref>, This is a review<ref>{{Cite journal|last=Kramer|first=Susanne|last2=McLennan|first2=Alexander G.|date=2019|title=The complex enzymology of mRNA decapping: Enzymes of four classes cleave pyrophosphate bonds|url=https://onlinelibrary.wiley.com/doi/abs/10.1002/wrna.1511|journal=WIREs RNA|language=en|volume=10|issue=1|pages=e1511|doi=10.1002/wrna.1511|issn=1757-7012}}</ref>, This is primary source about a specific protein in the complex<ref>{{Cite journal|last=Delorme-Axford|first=Elizabeth|last2=Abernathy|first2=Emma|last3=Lennemann|first3=Nicholas J.|last4=Bernard|first4=Amélie|last5=Ariosa|first5=Aileen|last6=Coyne|first6=Carolyn B.|last7=Kirkegaard|first7=Karla|last8=Klionsky|first8=Daniel J.|date=2018-05-04|title=The exoribonuclease Xrn1 is a post-transcriptional negative regulator of autophagy|url=https://doi.org/10.1080/15548627.2018.1441648|journal=Autophagy|volume=14|issue=5|pages=898–912|doi=10.1080/15548627.2018.1441648|issn=1554-8627|pmc=PMC6070002|pmid=29465287}}</ref>, This is one of the first articles discussing the degredation of mRNA and decapping complexes published on Pubmed<ref>{{Cite journal|last=Beelman|first=C. A.|last2=Parker|first2=R.|date=1995-04-21|title=Degradation of mRNA in eukaryotes|url=https://pubmed.ncbi.nlm.nih.gov/7736570/|journal=Cell|volume=81|issue=2|pages=179–183|doi=10.1016/0092-8674(95)90326-7|issn=0092-8674|pmid=7736570}}</ref> |
Sources for the article [[Decapping complex|Decapping Complex]]: This is a review<ref name=":0">{{Cite journal|last=Charenton|first=Clément|last2=Graille|first2=Marc|date=2018-12-19|title=mRNA decapping: finding the right structures|url=https://royalsocietypublishing.org/doi/10.1098/rstb.2018.0164|journal=Philosophical Transactions of the Royal Society B: Biological Sciences|volume=373|issue=1762|pages=20180164|doi=10.1098/rstb.2018.0164|pmc=PMC6232594|pmid=30397101}}</ref>, This is a review<ref>{{Cite journal|last=Kramer|first=Susanne|last2=McLennan|first2=Alexander G.|date=2019|title=The complex enzymology of mRNA decapping: Enzymes of four classes cleave pyrophosphate bonds|url=https://onlinelibrary.wiley.com/doi/abs/10.1002/wrna.1511|journal=WIREs RNA|language=en|volume=10|issue=1|pages=e1511|doi=10.1002/wrna.1511|issn=1757-7012}}</ref>, This is primary source about a specific protein in the complex<ref>{{Cite journal|last=Delorme-Axford|first=Elizabeth|last2=Abernathy|first2=Emma|last3=Lennemann|first3=Nicholas J.|last4=Bernard|first4=Amélie|last5=Ariosa|first5=Aileen|last6=Coyne|first6=Carolyn B.|last7=Kirkegaard|first7=Karla|last8=Klionsky|first8=Daniel J.|date=2018-05-04|title=The exoribonuclease Xrn1 is a post-transcriptional negative regulator of autophagy|url=https://doi.org/10.1080/15548627.2018.1441648|journal=Autophagy|volume=14|issue=5|pages=898–912|doi=10.1080/15548627.2018.1441648|issn=1554-8627|pmc=PMC6070002|pmid=29465287}}</ref>, This is one of the first articles discussing the degredation of mRNA and decapping complexes published on Pubmed<ref name=":1">{{Cite journal|last=Beelman|first=C. A.|last2=Parker|first2=R.|date=1995-04-21|title=Degradation of mRNA in eukaryotes|url=https://pubmed.ncbi.nlm.nih.gov/7736570/|journal=Cell|volume=81|issue=2|pages=179–183|doi=10.1016/0092-8674(95)90326-7|issn=0092-8674|pmid=7736570}}</ref> |
||
| Line 21: | Line 21: | ||
[[DCP2|Dcp2]] is the protein that actually decaps mRNA, and the rest of proteins in the complex enhance it's function and allow it to [[Hydrolysis|hydrolyze]] the mRNA [[Five-prime cap|5' cap]].<ref name=":0" /> |
[[DCP2|Dcp2]] is the protein that actually decaps mRNA, and the rest of proteins in the complex enhance it's function and allow it to [[Hydrolysis|hydrolyze]] the mRNA [[Five-prime cap|5' cap]].<ref name=":0" /> |
||
'''Why Decapping mRNA is Important (?)'''- |
'''Why Decapping mRNA is Important (?)'''-The fact is that [[Messenger RNA|mRNA]] needs to be degraded at some point, or else mRNA will keep floating around the cell and create unwanted proteins at random. The mRNA 5' cap is specifically designed to keep mRNA from being degraded before it can be used, and so needs to be removed from the mRNA so the mRNA decay pathway can take care of it.<ref name=":1" /> {{dashboard.wikiedu.org sandbox}} |
||
<references /> |
<references /> |
||
Revision as of 06:10, 13 November 2020
Sources for the article Decapping Complex: This is a review[1], This is a review[2], This is primary source about a specific protein in the complex[3], This is one of the first articles discussing the degredation of mRNA and decapping complexes published on Pubmed[4]
Organization ideas, likely to be scattered about the current, existing Decapping Complex:
Structure of the complex
The various subunits are called slightly different things depending on the organism they come from. [1]
This is what is currently written, anything italicized is not mine. But I've linked some things that were previously unlinked, and noted some things that I'm considering changing:
Yeast decapping complex
In yeast (S. cerevisiae), Dcp2 is joined by the decapping activator Dcp1, the helicase Dhh1, the exonuclease Xrn1, nonsense mediated decay factors Upf1, Upf2, and Upf3, the LSm complex, Pat1, and various other proteins. These proteins all localize to cytoplasmic structures called P-bodies. Notably in yeast there are no translation factors or ribosomal proteins inside P-bodies.
Metazoan decapping complex
Higher eukaryotes have slightly different members of the decapping complex. The enzyme Dcp2 is the main catalytic subunit, which forms a holoenzyme with Dcp1, and interacts with auxillary proteins such as Xrn1, Upf1, Upf2, Upf3, the LSm complex, and the Dhh1 ortholog Rck/p-54 to properly carry out its function. Proteins unique to plants and mammals include the beta propeller protein Hedls and the enhancer of decapping Edc3. Structural details of the assembly of this complex are not known, only physical association by immunoprecipitation.
How the Complex Decaps mRNA
Dcp2 is the protein that actually decaps mRNA, and the rest of proteins in the complex enhance it's function and allow it to hydrolyze the mRNA 5' cap.[1]
Why Decapping mRNA is Important (?)-The fact is that mRNA needs to be degraded at some point, or else mRNA will keep floating around the cell and create unwanted proteins at random. The mRNA 5' cap is specifically designed to keep mRNA from being degraded before it can be used, and so needs to be removed from the mRNA so the mRNA decay pathway can take care of it.[4]
 | This is a user sandbox of ExasperatedOctopus. You can use it for testing or practicing edits. This is not the sandbox where you should draft your assigned article for a dashboard.wikiedu.org course. To find the right sandbox for your assignment, visit your Dashboard course page and follow the Sandbox Draft link for your assigned article in the My Articles section. |
- ^ a b c Charenton, Clément; Graille, Marc (2018-12-19). "mRNA decapping: finding the right structures". Philosophical Transactions of the Royal Society B: Biological Sciences. 373 (1762): 20180164. doi:10.1098/rstb.2018.0164. PMC 6232594. PMID 30397101.
{{cite journal}}: CS1 maint: PMC format (link) - ^ Kramer, Susanne; McLennan, Alexander G. (2019). "The complex enzymology of mRNA decapping: Enzymes of four classes cleave pyrophosphate bonds". WIREs RNA. 10 (1): e1511. doi:10.1002/wrna.1511. ISSN 1757-7012.
- ^ Delorme-Axford, Elizabeth; Abernathy, Emma; Lennemann, Nicholas J.; Bernard, Amélie; Ariosa, Aileen; Coyne, Carolyn B.; Kirkegaard, Karla; Klionsky, Daniel J. (2018-05-04). "The exoribonuclease Xrn1 is a post-transcriptional negative regulator of autophagy". Autophagy. 14 (5): 898–912. doi:10.1080/15548627.2018.1441648. ISSN 1554-8627. PMC 6070002. PMID 29465287.
{{cite journal}}: CS1 maint: PMC format (link) - ^ a b Beelman, C. A.; Parker, R. (1995-04-21). "Degradation of mRNA in eukaryotes". Cell. 81 (2): 179–183. doi:10.1016/0092-8674(95)90326-7. ISSN 0092-8674. PMID 7736570.