Overexpression of PRMT6 does not suppress HIV-1 Tat transactivation in cells naturally lacking PRMT6

Virology Journal

Volumn 10, Issue , 2013, Pages

  Sivakumaran, Haran ^a   Lin, Min Hsuan ^a   Apolloni, Ann ^a   Cutillas, Vincent ^a   Jin, Hongping ^a   Li, Dongsheng ^a   Wei, Ting ^a   Harrich, David ^a  

^a QIMR BERGHOFER MEDICAL RESEARCH INSTITUTE   (Australia)

Author keywords

A549 cell line; HIV; Protein arginine methyltransferase 6; Protein methylation; Tat

Indexed keywords

PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 6; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CANCER CELL CULTURE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DOWN REGULATION; GENE EXPRESSION; GENE SEQUENCE; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; IMMUNOPRECIPITATION; PLASMID; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; STEADY STATE; VIRUS REPLICATION;

CELL LINE; EPITHELIAL CELLS; HIV-1; HOST-PATHOGEN INTERACTIONS; HUMANS; IMMUNOPRECIPITATION; NUCLEAR PROTEINS; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; PROTEIN-ARGININE N-METHYLTRANSFERASES; TAT GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS; TRANSCRIPTIONAL ACTIVATION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84879244886     PISSN: None     EISSN: 1743422X     Source Type: Journal    
DOI: 10.1186/1743-422X-10-207     Document Type: Article

References (44)

1. A novel CDK9-associated C-type cyclin interacts directly with HIV-1 tat and mediates its high-affinity, loop-specific binding to TAR RNA. Wei P, Garber ME, Fang SM, Fischer WH, Jones KA, Cell 1998 92 451 462 10.1016/S0092-8674(00) 80939-3 9491887
2. The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription. Yang Z, Zhu Q, Luo K, Zhou Q, Nature 2001 414 317 322 10.1038/35104575 11713532
3. Kick-sTARting HIV-1 transcription elongation by 7SK snRNP deporTATion. Barboric M, Lenasi T, Nat Struct Mol Biol 2010 17 928 930 10.1038/nsmb0810-928 20683478
4. RNA-mediated displacement of an inhibitory snRNP complex activates transcription elongation. D'Orso I, Frankel AD, Nat Struct Mol Biol 2010 17 815 821 10.1038/nsmb.1827 20562857
5. Recruitment and activation of RSK2 by HIV-1 Tat. Hetzer C, Bisgrove D, Cohen MS, Pedal A, Kaehlcke K, Speyerer A, Bartscherer K, Taunton J, Ott M, PLoS One 2007 2 151 10.1371/journal.pone.0000151 17225856
6. Methylation: a regulator of HIV-1 replication? Yedavalli VR, Jeang KT, Retrovirology 2007 4 9 10.1186/1742-4690-4-9 17274823
7. Methylation of tat by PRMT6 regulates human immunodeficiency virus type 1 gene expression. Boulanger MC, Liang C, Russell RS, Lin R, Bedford MT, Wainberg MA, Richard S, J Virol 2005 79 124 131 10.1128/JVI.79.1.124-131.2005 15596808
8. Lysine methylation of HIV-1 tat regulates transcriptional activity of the viral LTR. Van Duyne R, Easley R, Wu W, Berro R, Pedati C, Klase Z, Kehn-Hall K, Flynn EK, Symer DE, Kashanchi F, Retrovirology 2008 5 40 10.1186/1742-4690-5- 40 18498648
9. The Cellular lysine methyltransferase Set7/9-KMT7 binds HIV-1 TAR RNA, monomethylates the viral transactivator tat, and enhances HIV transcription. Pagans S, Kauder SE, Kaehlcke K, Sakane N, Schroeder S, Dormeyer W, Trievel RC, Verdin E, Schnolzer M, Ott M, Cell Host Microbe 2010 7 234 244 10.1016/j.chom.2010.02.005 20227666
10. Activation of HIV transcription by the viral tat protein requires a demethylation step mediated by lysine-specific demethylase 1 (LSD1/KDM1). Sakane N, Kwon HS, Pagans S, Kaehlcke K, Mizusawa Y, Kamada M, Lassen KG, Chan J, Greene WC, Schnoelzer M, Ott M, PLoS Pathog 2011 7 1002184 10.1371/journal.ppat. 1002184 21876670
11. Decoding tat: the biology of HIV tat posttranslational modifications. Hetzer C, Dormeyer W, Schnolzer M, Ott M, Microbes Infect 2005 7 1364 1369 10.1016/j.micinf.2005.06.003 16046164
12. Arginine methylation of the human immunodeficiency virus type 1 tat protein by PRMT6 negatively affects tat interactions with both cyclin T1 and the tat transactivation region. Xie B, Invernizzi CF, Richard S, Wainberg MA, J Virol 2007 81 4226 4234 10.1128/JVI.01888-06 17267505
13. Arginine methylation increases the stability of human immunodeficiency virus type 1 tat. Sivakumaran H, van der Horst A, Fulcher AJ, Apolloni A, Lin MH, Jans DA, Harrich D, J Virol 2009 83 11694 11703 10.1128/JVI.00499-09 19726520
14. The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans. Wolf SS, Cell Mol Life Sci 2009 66 2109 2121 10.1007/s00018-009-0010-x 19300908
15. Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. Guccione E, Bassi C, Casadio F, Martinato F, Cesaroni M, Schuchlautz H, Luscher B, Amati B, Nature 2007 449 933 937 10.1038/nature06166 17898714
16. PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation. Hyllus D, Stein C, Schnabel K, Schiltz E, Imhof A, Dou Y, Hsieh J, Bauer UM, Genes Dev 2007 21 3369 3380 10.1101/gad.447007 18079182
17. Arginine methylation of the histone H3 tail impedes effector binding. Iberg AN, Espejo A, Cheng D, Kim D, Michaud-Levesque J, Richard S, Bedford MT, J Biol Chem 2008 283 3006 3010 18077460
18. Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation. Kirmizis A, Santos-Rosa H, Penkett CJ, Singer MA, Vermeulen M, Mann M, Bahler J, Green RD, Kouzarides T, Nature 2007 449 928 932 10.1038/nature06160 17898715
19. PRMT6 diminishes HIV-1 Rev binding to and export of viral RNA. Invernizzi CF, Xie B, Richard S, Wainberg MA, Retrovirology 2006 3 93 10.1186/1742-4690-3- 93 17176473
20. Arginine methylation of the HIV-1 nucleocapsid protein results in its diminished function. Invernizzi CF, Xie B, Frankel FA, Feldhammer M, Roy BB, Richard S, Wainberg MA, AIDS 2007 21 795 805 10.1097/QAD.0b013e32803277ae 17415034
21. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. Frankel A, Yadav N, Lee J, Branscombe TL, Clarke S, Bedford MT, J Biol Chem 2002 277 3537 3543 10.1074/jbc.M108786200 11724789
22. Multiple functional domains of tat, the trans-activator of HIV-1, defined by mutational analysis. Kuppuswamy M, Subramanian T, Srinivasan A, Chinnadurai G, Nucleic Acids Res 1989 17 3551 3561 10.1093/nar/17.9.3551 2542902
23. Functional domains required for tat-induced transcriptional activation of the HIV-1 long terminal repeat. Garcia JA, Harrich D, Pearson L, Mitsuyasu R, Gaynor RB, EMBO J 1988 7 3143 3147 3181132
24. Functional analysis of the N-terminal domain of tat protein of the human immunodeficiency virus type 1. Reddy MV, Desai M, Jeyapaul J, Prasad DD, Seshamma T, Palmeri D, Khan SA, Oncogene 1992 7 1743 1748 1501886
25. Structural and functional characterization of human immunodeficiency virus tat protein. Ruben S, Perkins A, Purcell R, Joung K, Sia R, Burghoff R, Haseltine WA, Rosen CA, J Virol 1989 63 1 8 2535718
26. UniGene: a unified view of the transcriptome. Pontius JU, Wagner L, Schuler GD, The NCBI Handbook: National Center for Biotechnology Information, McEntyre J, Ostell J, Bethesda MD, 2003
27. In vitro cultivation of human tumors: establishment of cell lines derived from a series of solid tumors. Giard DJ, Aaronson SA, Todaro GJ, Arnstein P, Kersey JH, Dosik H, Parks WP, J Natl Cancer Inst 1973 51 1417 1423 4357758
28. Establishment and characterization of an epstein-barr virus (EBC)-negative lymphoblastoid B cell line (BJA-B) from an exceptional, EBV-genome-negative African burkitt's lymphoma. Menezes J, Leibold W, Klein G, Clements G, Biomedicine 1975 22 276 284 179629
29. A new mathematical model for relative quantification in real-time RT-PCR. Pfaffl MW, Nucleic Acids Res 2001 29 45 10.1093/nar/29.9.e45 11328886
30. Arginine methylation regulates DNA polymerase beta. El-Andaloussi N, Valovka T, Toueille M, Steinacher R, Focke F, Gehrig P, Covic M, Hassa PO, Schar P, Hubscher U, Hottiger MO, Mol Cell 2006 22 51 62 10.1016/j.molcel.2006.02.013 16600869
31. Thrombospondin-1 is a transcriptional repression target of PRMT6. Michaud-Levesque J, Richard S, J Biol Chem 2009 284 21338 21346 10.1074/jbc.M109.005322 19509293
32. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Zhang X, Cheng X, Structure 2003 11 509 520 10.1016/S0969-2126(03)00071-6 12737817
33. HIV-1 TAR RNA enhances the interaction between tat and cyclin T1. Zhang J, Tamilarasu N, Hwang S, Garber ME, Huq I, Jones KA, Rana TM, J Biol Chem 2000 275 34314 34319 10944537
34. HIV-1 tat assembles a multifunctional transcription elongation complex and stably associates with the 7SK snRNP. Sobhian B, Laguette N, Yatim A, Nakamura M, Levy Y, Kiernan R, Benkirane M, Mol Cell 2010 38 439 451 10.1016/j.molcel.2010.04.012 20471949
35. A quantitative proteomic analysis of lung epithelial (A549) cells infected with 2009 pandemic influenza a virus using stable isotope labelling with amino acids in cell culture. Dove BK, Surtees R, Bean TJ, Munday D, Wise HM, Digard P, Carroll MW, Ajuh P, Barr JN, Hiscox JA, Proteomics 2012 12 1431 1436 10.1002/pmic.201100470 22585751
36. Dysregulation of PRMT1 and PRMT6, type I arginine methyltransferases, is involved in various types of human cancers. Yoshimatsu M, Toyokawa G, Hayami S, Unoki M, Tsunoda T, Field HI, Kelly JD, Neal DE, Maehara Y, Ponder BA, et al. Int J Cancer 2011 128 562 573 10.1002/ijc.25366 20473859
37. Immune hyperactivation of HIV-1-infected T cells mediated by tat and the CD28 pathway. Ott M, Emiliani S, Van Lint C, Herbein G, Lovett J, Chirmule N, McCloskey T, Pahwa S, Verdin E, Science 1997 275 1481 1485 10.1126/science.275. 5305.1481 9045614
38. Acetylation of the HIV-1 tat protein by p300 is important for its transcriptional activity. Ott M, Schnolzer M, Garnica J, Fischle W, Emiliani S, Rackwitz HR, Verdin E, Curr Biol 1999 9 1489 1492 10.1016/S0960-9822(00)80120-7 10607594
39. Trans-activator gene of human T-lymphotropic virus type III (HTLV-III). Arya SK, Guo C, Josephs SF, Wong-Staal F, Science 1985 229 69 73 10.1126/science.2990040 2990040
40. Phosphatidylinositol-(4,5)-bisphosphate enables efficient secretion of HIV-1 tat by infected T-cells. Rayne F, Debaisieux S, Yezid H, Lin YL, Mettling C, Konate K, Chazal N, Arold ST, Pugniere M, Sanchez F, et al. EMBO J 2010 29 1348 1362 10.1038/emboj.2010.32 20224549
41. Tits and bits of HIV tat protein. Johri MK, Mishra R, Chhatbar C, Unni SK, Singh SK, Expert Opin Biol Ther 2011 11 269 283 10.1517/14712598.2011.546339 21204735
42. Potent inhibition of HIV-1 replication by a tat mutant. Meredith LW, Sivakumaran H, Major L, Suhrbier A, Harrich D, PLoS One 2009 4 7769 10.1371/journal.pone.0007769 19901984
43. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Bradford MM, Anal Biochem 1976 72 248 254 10.1016/0003-2697(76)90527-3 942051
44. Polypeptides of the tail fibres of bacteriophage T4. King J, Laemmli UK, J Mol Biol 1971 62 465 477 10.1016/0022-2836(71)90148-3 5136579