5'-3' exoribonuclease 2

Revision as of 21:47, 28 November 2016 by en>Alakey (→‎References: Adding link to XRN2 gene details page and display in UCSC genome browser.)
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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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5'-3' Exoribonuclease 2 (XRN2) also known as Dhm1-like protein is an exoribonuclease enzyme that in humans is encoded by the XRN2 gene.[1]

The human gene encoding XRN2 shares similarity with the mouse Dhm1 and the yeast's Dhp1 (Schizosaccharomyces pombe) or RAT1 (Saccharomyces) genes. The yeast gene is involved in homologous recombination and RNA metabolism, such as RNA synthesis and RNA trafficking and termination.[2] Complementation studies show that Dhm1 has a similar function in mouse as Dhp1.

Function

Human XRN2 is involved in the torpedo model of transcription termination.[3]

The C. elegans homologue, XRN-2, is involved in the degradation of certain mature miRNAs and their dislodging from miRISC miRNAs.[4]

In yeast, the Rat1 protein has been shown to also be involved in the torpedo transcription termination model. When a polyadenylation site has been detected on the nascent RNA and cleaved by the RNA polymerase II, the Rtt103 factor recruits Rat1 and attaches it to free end. The exonuclease activity of Rat1 degrades the RNA strand and halts transcriptions upon catching up to the polymerase.[2]

References

  1. Zhang M, Yu L, Xin Y, Hu P, Fu Q, Yu C, Zhao S (July 1999). "Cloning and mapping of the XRN2 gene to human chromosome 20p11.1-p11.2". Genomics. 59 (2): 252–4. doi:10.1006/geno.1999.5866. PMID 10409438.
  2. 2.0 2.1 David Tollervey (November 2004). "Termination by torpedo". Nature. 432: 456–457. doi:10.1038/432456a.
  3. West S, Gromak N, Proudfoot NJ (November 2004). "Human 5' --> 3' exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites". Nature. 432 (7016): 522–5. doi:10.1038/nature03035. PMID 15565158.
  4. Chatterjee S, Grosshans H (September 2009). "Active turnover modulates mature microRNA activity in Caenorhabditis elegans". Nature. 461 (7263): 546–9. doi:10.1038/nature08349. PMID 19734881.

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