Mitochondrial localization of the OAS1 p46 isoform associated with a common single nucleotide polymorphism

BMC Cell Biology

Volumn 15, Issue 1, 2014, Pages

  Kjær, Karina H ^a   Pahus, Jytte ^a   Hansen, Mariann F ^a   Poulsen, Jesper B ^a   Christensen, Erik I ^a   Justesen, Just ^a   Martensen, Pia M ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

2' 5' Oligoadenylate synthetase (OAS); Diabetes; Mitochondria; Single nucleotide polymorphism (SNP)

Indexed keywords

GLYCINE; INTERFERON; ISOPROTEIN; MESSENGER RNA; MITOCHONDRIAL PROTEIN; PROTEIN OAS1; PROTEIN P42; PROTEIN P46; PROTEIN P48; PROTEIN P52; SERINE; UNCLASSIFIED DRUG; 2',5' OLIGOADENYLATE SYNTHETASE; OAS1 PROTEIN, HUMAN;

ALLELE; AMINO ACID SEQUENCE; ARTICLE; CELL VACUOLE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; DAUDI CELL LINE; ENZYME ACTIVITY; GENE; HELA CELL LINE; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; LYSOSOME; MITOCHONDRION; OAS1 P46 GENE; OAS1 P48 GENE; OAS1 P52 GENE; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; RNA SPLICING; SINGLE NUCLEOTIDE POLYMORPHISM; CELL LINE; CHEMISTRY; GENE EXPRESSION; GENETICS; METABOLISM;

2',5'-OLIGOADENYLATE SYNTHETASE; CELL LINE; GENE EXPRESSION; HUMANS; MITOCHONDRIA; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEIN ISOFORMS; RNA, MESSENGER;

EID: 84907288937     PISSN: None     EISSN: 14712121     Source Type: Journal    
DOI: 10.1186/1471-2121-15-33     Document Type: Article

References (43)

1. Sadler AJ, Williams BRG. Interferon-inducible antiviral effectors. Nat Rev Immunol 2008, 8:559-568. 10.1038/nri2314, 2522268, 18575461.
2. Randall RE, Goodbourne S. Interferons and viruses: an interplay between induction, signalling, antiviral responses and virus countermeasures. J Gen Virol 2008, 89:1-47. 10.1099/vir.0.83391-0, 18089727.
3. Hovanessian AG, Justesen J. The human 2′-5′oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2′-5′ instead of 3′-5′ phosphodiester bond formation. Biochimie 2007, 89(6-7):779-788.
4. Justesen J, Hartmann R, Kjeldgaard NO. Gene structure and function of the 2′-5′-oligoadenylate synthetase family. Cell Mol Life Sci 2000, 57(11):1593-1612. 10.1007/PL00000644, 11092454.
5. Marie I, Hovanessian AG. The 69-kDa 2-5A synthetase is composed of two homologous and adjacent functional domains. J Biol Chem 1992, 267(14):9933-9939.
6. Chebath J, Benech P, Hovanessian A, Galabru J, Revel M. Four different forms of interferon-induced 2′,5′-oligo(A) synthetase identified by immunoblotting in human cells. J Biol Chem 1987, 262(8):3852-3857.
7. Hovanessian AG, Laurent AG, Chebath J, Galabru J, Robert N, Svab J. Identification of 69-kd and 100-kd forms of 2-5A synthetase in interferon-treated human cells by specific monoclonal antibodies. EMBO J 1987, 6(5):1273-1280. 553929, 2440675.
8. Ghosh A, Sakar SN, Rowe TM, Sen GC. A specific isozyme of 2′-5′ Oligoadenylate synthetase is a dual function proapoptotic protein of the Bcl-2 family. J Biol Chem 2001, 276:25447-25455. 10.1074/jbc.M100496200, 11323417.
9. Bonnevie-Nielsen V, Field LL, Lu S, Zheng DJ, Li M, Martensen PM, Nielsen TB, Beck-Nielsen H, Lau YL, Pociot F. Variation in antiviral 2′,5′-oligoadenylate synthetase (2′5′AS) enzyme activity is controlled by a single-nucleotide polymorphism at a splice-acceptor site in the OAS1 gene. Am J Hum Genet 2005, 76(4):623-633. 10.1086/429391, 1199299, 15732009.
10. Noguchi S, Hamano E, Matsushita I, Hijikata M, Ito H, Nagase T, Keicho N. Differential effects of a common splice site polymorphism on the generation of OAS1 variants in human bronchial epithelial cells. Hum Immunol 2013, 74:395-401. 10.1016/j.humimm.2012.11.011, 23220500.
11. Besse S, Rebouillat D, Marie I, Puvion-Dutilleul F, Hovanessian AG. Ultrastructural localization of interferon-inducible double-stranded RNA-activated enzymes in human cells. Exp Cell Res 1998, 239(2):379-392. 10.1006/excr.1997.3908, 9521856.
12. Rebouillat D, Hovanain A, Marie I, Hovanessian AG. The 100-kDa 2′,5′-oligoadenylate synthetase catalysing preferentially the synthesis of dimeric pppA2′p5′A molecules is composed of three homologous domains. J Biol Chem 1999, 274:1557-1565. 10.1074/jbc.274.3.1557, 9880533.
13. Benech P, Mory Y, Revel M, Chebath J. Structure of two forms of the interferon-induced (2′-5′) oligo A synthetase of human cells based on cDNAs and gene sequences. EMBO J 1985, 4(9):2249-2256. 554493, 2416561.
14. Field LL, Bonnevie-Nielsen V, Pociot F, Lu S, Nielsen TB, Beck-Nielsen H. OAS1 splice site polymorphism controlling antiviral enzyme activity influences susceptibility to type 1 diabetes. Diabetes 2005, 54:1588-1591. 10.2337/diabetes.54.5.1588, 15855350.
15. Tessier MC, Qu HQ, Frechette R, Bacot F, Grabs R, Taback SP, Lawson ML, Kirsch SE, Hudson TJ, Polychronakos C. Type 1 diabetes and the OAS gene cluster: association with splicing polymorphism or haplotype?. J Med Genet 2006, 43(2):129-132. 2564627, 16014697.
16. Smyth DJ, Cooper JD, Lowe CE, Nutland S, Walker NM, Clayton DG, Todd JA. No evidence for association of OAS1 with Type 1 diabetes in unaffected siblings or Type 1 diabetic cases. Diabetes 2006, 55:1525-1528. 10.2337/db05-1452, 16644715.
17. Qu HQ, Polychronakos C. Reassessment of the type I diabetes association of the OAS1 locus. Genes Immun 2009, 10(Suppl 1):S69-S73. 2805449, 19956105.
18. Fedetz M, Matesanz F, Caro-Maldonado A, Fernandez O, Tamayo JA, Guerrero M, Delgado C, Lopez-Guerrero JA, Alcina A. OAS1 gene haplotype confers susceptibility to multiple sclerosis. Tissue Antigens 2006, 68(5):446-449. 10.1111/j.1399-0039.2006.00694.x, 17092260.
19. O'Brien M, Lonergan R, Costelloe L, O'Rourke K, Fletcher JI, Kinsella K, Sweeney C, Antonelli G, Mills KH, O'Farrelly C, Hutchinson M, Tubridy N. OAS1. A multiple sclerosis susceptibility gene that influences disease severity. Neurology 2010, 75:411-418. 10.1212/WNL.0b013e3181ebdd2b, 20679634.
20. Cagliani R, Fumagalli M, Guerini FR, Riva S, Galimberti D, Comi GP, Agliardi C, Scarpini E, Pozzoli U, Forni D, Caputo D, Asselta R, Biasin M, Paraboschi EM, Bresolin N, Clerici M, Sironi M. Identification of a new susceptibility variant for multiple sclerosis in OAS1 by population genetics analysis. Hum Genet 2012, 131:87-97. 10.1007/s00439-011-1053-2, 21735172.
21. Haralambieva IH, Ovsyannikova IG, Umlauf BJ, Vierkant RA, Pankratz VS, Jacobson RM, Poland GA. Genetic polymorphims in host antiviral genes: Associations with humoral and cellular immunity to measels vaccine. Vaccine 2011, 29:8988-8997. 10.1016/j.vaccine.2011.09.043, 3941984, 21939710.
22. Haralambieva IH, Dhiman N, Ovsyannikova IG, Vierkant RA, Pankratz VS, Jacobson RM, Poland GA. 2′-5′-Oligoadenylate synthetase single-nucleotide polymorphisms and haplotypes are associated with variations in immune responses to rubella vaccine. Hum Immunol 2010, 71(4):383-391. 10.1016/j.humimm.2010.01.004, 2842477, 20079393.
23. Lim JK, Lisco A, McDermott DH, Huynh L, Ward JM, Johnson B, Johnson H, Pape J, Foster GA, Krysztof D, Follmann D, Stramer SL, Margolis LB, Murphy PM. Genetic variation in OAS1 is a risk factor for initial infection with West Nile virus in man. PLoS Pathog 2009, 5(2):e1000321. 10.1371/journal.ppat.1000321, 2642680, 19247438.
24. Bigham AW, Buckingham KJ, Husain S, Emond MJ, Bofferding KM, Gildersleeve H, Rutherford A, Astakhova NM, Perelygin AA, Busch MP, Murray KO, Sejvar JJ, Green S, Kriesel J, Brinton MA, Bamshad M. Host genetic risk factors for West Nile Virus infection and disease progression. PLoS One 2011, 6:e2475.
25. Awady MKE, Anany MA, Esmat G, Zayed N, Tabll AA, Helmy A, Zayady AR, Abdalla MS, Sharada HM, Raziky ME, Akel WE, Abdalla S, Din NGBE. Single nucleotide polymorphism at exon 7 splice acceptor site of OAS1 gene determines response of hepatitis C virus patients to interferon therapy. J Gastroenterol Hepatol 2011, 26:843-850. 10.1111/j.1440-1746.2010.06605.x, 21182542.
26. Kwon Y-C, Kang J-I, Hwang SB, Ahn B-Y. The ribonuclease L-dependent antiviroal roles of human 2′,5′-oligoadenylate synthetase family members against hepatitis C virus. FEBS Lett 2013, 587:156-164. 10.1016/j.febslet.2012.11.010, 23196181.
27. Lin R-J, Yu H-P, Chang B-L, Tang W-C, Liao C-L, Lin Y-L. Distinct antiviral roles for human 2′,5′-oligoadenylate synthetase family members against dengue virus infection. J Immunol 2009, 183:8035-8043. 10.4049/jimmunol.0902728, 19923450.
28. Witt PL, Marié I, Robert N, Irizarry A, Borden EC, Hovanessian AG. Isoforms p69 and p100 of 2′,5′-oligoadenylate synthetase induced differentially by interferons in vivo and in vitro. J Interferon Res 1993, 13:17-23. 10.1089/jir.1993.13.17, 8454907.
29. Poulsen JB, Andersen KR, Kjaer KH, Durand F, Faou P, Vestergaard AL, Talbo GH, Hoogenraad N, Brodersen DE, Justesen J, Martensen PM. Human 2′-phosphodiesterase localizes to the mitochondrial matrix with a putative function in mitochondrial RNA turnover. Nucleic Acids Res 2011, 39(9):3754-3770. 10.1093/nar/gkq1282, 3089451, 21245038.
30. Benech P, Merlin G, Revel M, Chebath J. 3′ end structure of the human (2′-5′) oligo A synthetase gene: prediction of two distinct proteins with cell type-specific expression. Nucl Acid Res 1985, 13(4):1267-1281.
31. Khanna KK, An SJ, Wu JM, Landolfo S, Hovanessian AG. Absence of the 40-kDa form of (2′-5′)oligoadenylate synthetase and its corresponding mRNA from skin fibroblasts derived from Alzheimer disease patients. Proc Natl Acad Sci U S A 1991, 88(13):5852-5856. 10.1073/pnas.88.13.5852, 51976, 1712108.
32. Tait SWG, Green DR. Mitochondria and cell death: Outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 2010, 11:621-632. 10.1038/nrm2952, 20683470.
33. Kjaer KH, Poulsen JB, Reintamm T, Saby E, Martensen PM, Kelve M, Justesen J. Evolution of the 2′-5′-oligoadenylate synthetase family in eukaryotes and bacteria. J Mol Evol 2009, 69(6):612-624. 10.1007/s00239-009-9299-1, 19904482.
34. Lane KT, Beese LS. Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. J Lipid Res 2006, 47(4):681-699. 10.1194/jlr.R600002-JLR200, 16477080.
35. Le Roy F, Bisbal C, Silhol M, Martinand C, Lebleu B, Salehzada T. The 2-5A/RNase L/RNase L inhibitor (RLI) [correction of (RNI)] pathway regulates mitochondrial mRNAs stability in interferon alpha-treated H9 cells. J Biol Chem 2001, 276(51):48473-48482.
36. Floyd-Smith G, Yoshie O, Lengyel P. Interferon action. Covalent linkage of (2′-5′)pppApApA(32P)pCp to (2′-5′) (A)n-dependent ribonucleases in cell extracts by ultraviolet irradiation. J Biol Chem 1982, 257(15):8584-8587.
37. Bayard BA, Gabrion JB. 2′,5′-Oligoadenylate-dependent RNAse located in nuclei: biochemical characterization and subcellular distribution of the nuclease in human and murine cells. Biochem J 1993, 296(Pt 1):155-160. 1137668, 8250837.
38. Rorbach J, Nicholls TJ, Minczuk M. PDE12 removes mitochondrial RNA poly(A) tails and controls translation in human mitochondria. Nucleic Acids Res 2011, 39(17):7750-7763. 10.1093/nar/gkr470, 3177208, 21666256.
39. Le Roy F, Silhol M, Salehzada T, Bisbal C. Regulation of mitochondrial mRNA stability by RNase L is translation-dependent and controls IFNalpha-induced apoptosis. Cell Death Differ 2007, 14(8):1406-1413. 10.1038/sj.cdd.4402130, 17431428.
40. Reed SE, Staley EM, Mayginnes JP, Pinel DJ, Tullis GE. Transfection of mammalian cells using linear polyethylenimine is a simple and effective means of producing recombiant adeno-associated virus vectors. J Virol Methods 2006, 138:85-98. 10.1016/j.jviromet.2006.07.024, 16950522.
41. Pfaffl MW. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 2001, 29(9):e45. 10.1093/nar/29.9.e45, 55695, 11328886.
42. Saby E, Poulsen JB, Justesen J, Kelve M, Uriz MJ. 2′-phosphodiesterase and 2′,5′-oligoadenylate synthetase activities in the lowest metazoans, sponge [porifera]. Biochimie 2009, 91:1531-1534. 10.1016/j.biochi.2009.07.015, 19665065.
43. Schneider CA, Rasband WS, Eliceiri KW. NIH Image to ImageJ: 25 years of image analysis. Nat Methods 2012, 9:671-675. 10.1038/nmeth.2089, 22930834.