The printable version is no longer supported and may have rendering errors. Please update your browser bookmarks and please use the default browser print function instead.
Poly(A)-specific ribonuclease (PARN), also known as polyadenylate-specific ribonuclease or deadenylating nuclease (DAN), is an enzyme that in humans is encoded by the PARNgene.[1][2]
Function
Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. The amino acid sequence of poly(A)-specific ribonuclease shows homology to the RNase D family of 3'-exonucleases. The protein appears to be localized in both the nucleus and the cytoplasm. It is not stably associated with polysomes or ribosomal subunits.[2] Hereditary mutations in PARN lead to the bone marrow failure disease Dyskeratosis Congenita which is caused by defective telomerase RNA processing and degradation in patients.[3][4][5][6][7][8][9]
↑Dhanraj S, Gunja SM, Deveau AP, Nissbeck M, Boonyawat B, Coombs AJ, Renieri A, Mucciolo M, Marozza A, Buoni S, Turner L, Li H, Jarrar A, Sabanayagam M, Kirby M, Shago M, Pinto D, Berman JN, Scherer SW, Virtanen A, Dror Y (November 2015). "Bone marrow failure and developmental delay caused by mutations in poly(A)-specific ribonuclease (PARN)". Journal of Medical Genetics. 52 (11): 738–48. doi:10.1136/jmedgenet-2015-103292. PMID26342108.
↑Tseng CK, Wang HF, Burns AM, Schroeder MR, Gaspari M, Baumann P (December 2015). "Human Telomerase RNA Processing and Quality Control". Cell Reports. 13 (10): 2232–43. doi:10.1016/j.celrep.2015.10.075. PMID26628367.
↑Nguyen D, Grenier St-Sauveur V, Bergeron D, Dupuis-Sandoval F, Scott MS, Bachand F (December 2015). "A Polyadenylation-Dependent 3' End Maturation Pathway Is Required for the Synthesis of the Human Telomerase RNA". Cell Reports. 13 (10): 2244–57. doi:10.1016/j.celrep.2015.11.003. PMID26628368.
Körner CG, Wahle E (April 1997). "Poly(A) tail shortening by a mammalian poly(A)-specific 3'-exoribonuclease". The Journal of Biological Chemistry. 272 (16): 10448–56. doi:10.1074/jbc.272.16.10448. PMID9099687.
Martinez J, Ren YG, Thuresson AC, Hellman U, Astrom J, Virtanen A (August 2000). "A 54-kDa fragment of the Poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting Poly(A)-specific 3' exonuclease". The Journal of Biological Chemistry. 275 (31): 24222–30. doi:10.1074/jbc.M001705200. PMID10801819.
Martînez J, Ren YG, Nilsson P, Ehrenberg M, Virtanen A (July 2001). "The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation". The Journal of Biological Chemistry. 276 (30): 27923–9. doi:10.1074/jbc.M102270200. PMID11359775.
Chen CY, Gherzi R, Ong SE, Chan EL, Raijmakers R, Pruijn GJ, Stoecklin G, Moroni C, Mann M, Karin M (November 2001). "AU binding proteins recruit the exosome to degrade ARE-containing mRNAs". Cell. 107 (4): 451–64. doi:10.1016/S0092-8674(01)00578-5. PMID11719186.
Ren YG, Martínez J, Virtanen A (February 2002). "Identification of the active site of poly(A)-specific ribonuclease by site-directed mutagenesis and Fe(2+)-mediated cleavage". The Journal of Biological Chemistry. 277 (8): 5982–7. doi:10.1074/jbc.M111515200. PMID11742007.
Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (January 2002). "Directed proteomic analysis of the human nucleolus". Current Biology. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID11790298.
Ren YG, Kirsebom LA, Virtanen A (November 2004). "Coordination of divalent metal ions in the active site of poly(A)-specific ribonuclease". The Journal of Biological Chemistry. 279 (47): 48702–6. doi:10.1074/jbc.M403858200. PMID15358788.
