XRN1 (gene): Difference between revisions
Content deleted Content added
m Anthony Appleyard moved page 5'-3' exoribonuclease 1 to XRN1 (gene): histmerge |
Citation bot (talk | contribs) Add: hdl, doi. | Use this bot. Report bugs. | Suggested by Whoop whoop pull up | #UCB_webform 386/3464 |
||
| (16 intermediate revisions by 9 users not shown) | |||
| Line 1: | Line 1: | ||
{{Infobox_gene}} |
|||
{{protein |
|||
| ⚫ | |||
|caption= |
|||
|image= |
|||
|width= |
|||
|HGNCid=30654 |
|||
|Symbol=XRN1 |
|||
|AltSymbols= |
|||
|EntrezGene=54464 |
|||
|OMIM=607994 |
|||
|RefSeq=NM_019001 |
|||
|UniProt=Q8IZH2 |
|||
|PDB= |
|||
|ECnumber= |
|||
|Chromosome=3 |
|||
|Arm=q |
|||
|Band=23 |
|||
|LocusSupplementaryData= |
|||
}} |
|||
| ⚫ | ''' |
||
| ⚫ | '''5′-3′ exoribonuclease 1''' ('''Xrn1''') is a [[protein]] that in humans is encoded by the XRN1 [[gene]]. Xrn1 [[Hydrolysis|hydrolyses]] [[RNA]] in the 5′ to 3′ [[Directionality (molecular biology)|direction]].<ref>{{cite journal | vauthors = Mullen TE, Marzluff WF | title = Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5' | journal = Genes & Development | volume = 22 | issue = 1 | pages = 50–65 | date = January 2008 | pmid = 18172165 | pmc = 2151014 | doi = 10.1101/gad.1622708 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: 5'-3' exoribonuclease 1 | url = https://www.ncbi.nlm.nih.gov/gene/54464 }}</ref> |
||
| ⚫ | |||
{{Reflist}} |
|||
== |
== Function == |
||
* {{MeshName|XRN1+protein,+human}} |
|||
This gene encodes a member of the 5′-3′ [[exonuclease]] family. The encoded protein may be involved in replication-dependent [[histone]] [[Messenger RNA|mRNA]] degradation, and interacts directly with the enhancer of [[Messenger RNA decapping|mRNA-decapping]] protein 4. In addition to mRNA metabolism, a similar protein in yeast has been implicated in a variety of nuclear and cytoplasmic functions, including [[eukaryotic_transcription|transcription]], [[eukaryotic translation|translation]], [[homologous recombination]], [[meiosis]], [[telomere]] maintenance, and [[microtubule]] assembly. Mutations in this gene are associated with [[osteosarcoma]], suggesting that the encoded protein may also play a role in [[bone formation]]. [[Alternative splicing]] results in multiple transcript variants. |
|||
[[Category:EC 3.1]] |
|||
==See also== |
|||
| ⚫ | |||
| ⚫ | |||
| ⚫ | |||
{{reflist}} |
|||
== Further reading == |
|||
{{refbegin | 2}} |
|||
* {{cite journal | vauthors = Bashkirov VI, Scherthan H, Solinger JA, Buerstedde JM, Heyer WD | title = A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates | journal = The Journal of Cell Biology | volume = 136 | issue = 4 | pages = 761–73 | date = February 1997 | pmid = 9049243 | pmc = 2132493 | doi = 10.1083/jcb.136.4.761}} |
|||
* {{cite journal | vauthors = Ingelfinger D, Arndt-Jovin DJ, Lührmann R, Achsel T | title = The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci | journal = RNA | volume = 8 | issue = 12 | pages = 1489–501 | date = December 2002 | doi = 10.1017/S1355838202021726 | pmid = 12515382 | pmc = 1370355 | hdl = 11858/00-001M-0000-0012-F270-9 | url = https://rnajournal.cshlp.org/content/8/12/1489.short }} |
|||
* {{cite journal | vauthors = Braun JE, Truffault V, Boland A, Huntzinger E, Chang CT, Haas G, Weichenrieder O, Coles M, Izaurralde E | title = A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradation | journal = Nature Structural & Molecular Biology | volume = 19 | issue = 12 | pages = 1324–31 | date = December 2012 | pmid = 23142987 | doi = 10.1038/nsmb.2413 | s2cid = 1134057 }} |
|||
* {{cite journal | vauthors = Li Y, Masaki T, Yamane D, McGivern DR, Lemon SM | title = Competing and noncompeting activities of miR-122 and the 5' exonuclease Xrn1 in regulation of hepatitis C virus replication | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 110 | issue = 5 | pages = 1881–6 | date = January 2013 | pmid = 23248316 | pmc = 3562843 | doi = 10.1073/pnas.1213515110 | doi-access = free }} |
|||
* {{cite journal | vauthors = Li Y, Yamane D, Lemon SM | title = Dissecting the roles of the 5' exoribonucleases Xrn1 and Xrn2 in restricting hepatitis C virus replication | journal = Journal of Virology | volume = 89 | issue = 9 | pages = 4857–65 | date = May 2015 | pmid = 25673723 | pmc = 4403451 | doi = 10.1128/JVI.03692-14 }} |
|||
* {{cite journal | vauthors = Burgess HM, Mohr I | title = Cellular 5'-3' mRNA exonuclease Xrn1 controls double-stranded RNA accumulation and anti-viral responses | journal = Cell Host & Microbe | volume = 17 | issue = 3 | pages = 332–44 | date = March 2015 | pmid = 25766294 | pmc = 4826345 | doi = 10.1016/j.chom.2015.02.003 }} |
|||
* {{cite journal | vauthors = Ding M, Lin B, Li T, Liu Y, Li Y, Zhou X, Miao M, Gu J, Pan H, Yang F, Li T, Liu XY, Li R | title = A dual yet opposite growth-regulating function of miR-204 and its target XRN1 in prostate adenocarcinoma cells and neuroendocrine-like prostate cancer cells | journal = Oncotarget | volume = 6 | issue = 10 | pages = 7686–700 | date = April 2015 | pmid = 25797256 | pmc = 4480709 | doi = 10.18632/oncotarget.3480 }} |
|||
* {{cite journal | vauthors = Blasco-Moreno B, de Campos-Mata L, Böttcher R, García-Martínez J, Jungfleisch J, Nedialkova DD, Chattopadhyay S, Gas ME, Oliva B, Pérez-Ortín JE, Leidel SA, Choder M, Díez J | title = The exonuclease Xrn1 activates transcription and translation of mRNAs encoding membrane proteins | journal = Nature Communications| volume = 21 | issue = 10 | pages = 1298 | date = March 2019 | pmid = 30899024 | pmc = 6428865 | doi = 10.1038/s41467-019-09199-6 | bibcode = 2019NatCo..10.1298B }} |
|||
{{refend}} |
|||
{{NLM content}} |
|||
| ⚫ | |||
Latest revision as of 05:39, 13 October 2022
5′-3′ exoribonuclease 1 (Xrn1) is a protein that in humans is encoded by the XRN1 gene. Xrn1 hydrolyses RNA in the 5′ to 3′ direction.[5][6]
Function
[edit]This gene encodes a member of the 5′-3′ exonuclease family. The encoded protein may be involved in replication-dependent histone mRNA degradation, and interacts directly with the enhancer of mRNA-decapping protein 4. In addition to mRNA metabolism, a similar protein in yeast has been implicated in a variety of nuclear and cytoplasmic functions, including transcription, translation, homologous recombination, meiosis, telomere maintenance, and microtubule assembly. Mutations in this gene are associated with osteosarcoma, suggesting that the encoded protein may also play a role in bone formation. Alternative splicing results in multiple transcript variants.
See also
[edit]References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000114127 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032410 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Mullen TE, Marzluff WF (January 2008). "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'". Genes & Development. 22 (1): 50–65. doi:10.1101/gad.1622708. PMC 2151014. PMID 18172165.
- ^ "Entrez Gene: 5'-3' exoribonuclease 1".
Further reading
[edit]- Bashkirov VI, Scherthan H, Solinger JA, Buerstedde JM, Heyer WD (February 1997). "A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates". The Journal of Cell Biology. 136 (4): 761–73. doi:10.1083/jcb.136.4.761. PMC 2132493. PMID 9049243.
- Ingelfinger D, Arndt-Jovin DJ, Lührmann R, Achsel T (December 2002). "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci". RNA. 8 (12): 1489–501. doi:10.1017/S1355838202021726. hdl:11858/00-001M-0000-0012-F270-9. PMC 1370355. PMID 12515382.
- Braun JE, Truffault V, Boland A, Huntzinger E, Chang CT, Haas G, Weichenrieder O, Coles M, Izaurralde E (December 2012). "A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradation". Nature Structural & Molecular Biology. 19 (12): 1324–31. doi:10.1038/nsmb.2413. PMID 23142987. S2CID 1134057.
- Li Y, Masaki T, Yamane D, McGivern DR, Lemon SM (January 2013). "Competing and noncompeting activities of miR-122 and the 5' exonuclease Xrn1 in regulation of hepatitis C virus replication". Proceedings of the National Academy of Sciences of the United States of America. 110 (5): 1881–6. doi:10.1073/pnas.1213515110. PMC 3562843. PMID 23248316.
- Li Y, Yamane D, Lemon SM (May 2015). "Dissecting the roles of the 5' exoribonucleases Xrn1 and Xrn2 in restricting hepatitis C virus replication". Journal of Virology. 89 (9): 4857–65. doi:10.1128/JVI.03692-14. PMC 4403451. PMID 25673723.
- Burgess HM, Mohr I (March 2015). "Cellular 5'-3' mRNA exonuclease Xrn1 controls double-stranded RNA accumulation and anti-viral responses". Cell Host & Microbe. 17 (3): 332–44. doi:10.1016/j.chom.2015.02.003. PMC 4826345. PMID 25766294.
- Ding M, Lin B, Li T, Liu Y, Li Y, Zhou X, Miao M, Gu J, Pan H, Yang F, Li T, Liu XY, Li R (April 2015). "A dual yet opposite growth-regulating function of miR-204 and its target XRN1 in prostate adenocarcinoma cells and neuroendocrine-like prostate cancer cells". Oncotarget. 6 (10): 7686–700. doi:10.18632/oncotarget.3480. PMC 4480709. PMID 25797256.
- Blasco-Moreno B, de Campos-Mata L, Böttcher R, García-Martínez J, Jungfleisch J, Nedialkova DD, Chattopadhyay S, Gas ME, Oliva B, Pérez-Ortín JE, Leidel SA, Choder M, Díez J (March 2019). "The exonuclease Xrn1 activates transcription and translation of mRNAs encoding membrane proteins". Nature Communications. 21 (10): 1298. Bibcode:2019NatCo..10.1298B. doi:10.1038/s41467-019-09199-6. PMC 6428865. PMID 30899024.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
 | This article on a gene on human chromosome 3 is a stub. You can help Wikipedia by expanding it. |