Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA

Journal of Cell Biology

Volumn 148, Issue 2, 2000, Pages 283-292

  Boisvert, François Michel ^a   Hendzel, Michael J ^a,b   Bazett Jones, David P ^a  

^a Dept of Cell Biology and Anatomy ^*  (Canada)

^b UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Acetylated chromatin; Correlative microscopy; Electron spectroscopic imaging; Nuclear structure; Transcription

Indexed keywords

ARTICLE; CARCINOGENESIS; CELL NUCLEUS INCLUSION BODY; CHROMATIN; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROMYELOCYTIC LEUKEMIA; PROTEIN STRUCTURE; RNA SYNTHESIS; RNA TRANSCRIPTION; SPECTROSCOPY; TRANSMISSION ELECTRON MICROSCOPY; VIRUS INFECTION;

ACETYLATION; CELL NUCLEUS; CHROMATIN; FLUORESCENT ANTIBODY TECHNIQUE; IMAGE PROCESSING, COMPUTER-ASSISTED; LEUKEMIA, PROMYELOCYTIC, ACUTE; MICROSCOPY, ELECTRON; MICROTOMY; NEOPLASM PROTEINS; NITROGEN; ORGANOMETALLIC COMPOUNDS; PHOSPHORUS; RNA, NEOPLASM; RNA, NUCLEAR; SPECTRUM ANALYSIS; STAINING AND LABELING;

DINOPHYCEAE; GYMNODINIUM; GYRODINIUM;

EID: 0034707690     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.148.2.283     Document Type: Article

References (51)

1. Ascoli, C.A., and G.G. Maul. 1991. Identification of a novel nuclear domain. J. Cell Biol. 112:785-795.
2. Bazett-Jones, D.P., and M.J. Hendzel. 1999. Electron spectroscopic imaging of chromatin. Companion Meth. Enzymol. 17:188-200.
3. Bazett-Jones, D.P., M.J. Hendzel, and M.J. Kruhlak. 1999. Stoichiometric analysis of protein- and nucleic acid-based structures in the cell nucleus. Micron. 30:151-157.
4. Bernhard, W. 1969. A new staining procedure for electron microscopical cytology. J. Ultrastruct. Res. 27:250-265.
5. Boggs, B.A., B. Connors, R.E. Sobel, A.C. Chinaud, and C.D. Allis. 1996. Reduced levels of histone H3 acetylation on the inactive X chromosomes as shown by histone acetylation. Chromosoma. 105:41-49.
6. Borrow, J., A.D. Goddard, D. Sheer, and E. Solomon. 1990. Molecular analysis of acute promyelocytic leukemia breakpoint cluster region on chromosome 17. Science. 249:1577-1580.
7. Chang, K.S., Y.-H. Fan, M. Andreeff, J. Liu, and Z.-M. Mu. 1995. The PML gene encodes a phosphoprotein associated with the nuclear matrix. Blood. 85:3646-3653.
8. Chelbi-Alix, M.K., L. Pelicano, F. Quignon, M.H.M. Koken, L. Venturini, M. Stadler, J. Pavlovic, L. Degos, and H. de The. 1995. Induction of the PML protein by interferons in normal and APL cells. Leukemia. 9:2027-2033.
9. Chen, T., F.-M. Boisvert, D.P. Bazett-Jones, and S. Richard. 1999. A role for the GSG domain in localizing Sam68 to novel nuclear structures in cancer cell lines. Mol. Biol. Cell. 10:3015-3033.
10. De Bruyn-Kops, A., and D.M. Knipe. 1994. Preexisting nuclear architecture defines the intranuclear location of herpes virus DNA replication structures. J. Virol. 68:3512-3526.
11. De Graaf, A., B.M. Humbel, N. Stuurman, P.M.P. van Bergen en Henegouwen, and A.J. Verkleij. 1992. Three-dimensional immunogold labeling of nuclear matrix proteins in permeabilized cells. Cell Biol. Int. Rep. 16:827-836.
12. de The, H., C. Chomienne, M. Lanotte, L. Degos, and A. Dejean. 1990. The t(15;17) translocation of acute promyelocytic leukaemia fuses the retinoic acid receptor alpha gene to a novel transcribed locus. Nature. 347:558-561.
13. de The, H., C. Lavau, A. Marchio, C. Chomienne, L. Degos, and A. Dejean. 1991. The PML-RAR alpha fusion mRNA generated by the 1(15:17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell. 66:675-684.
14. Desbois, C., R. Rousset, F. Bantignies, and P. Jalinot. 1996. Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I tax oncoprotein. Science. 273:951-953.
15. Doucas, V., A.M. Ishov, A. Romo, H. Juguilon, M.D. Weitzman, R.M. Evans, and G.G. Maul. 1996. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev. 111:196-207.
16. Doucas, V., M. Tini, D.A. Egan, and R.M. Evans. 1999. Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc. Null Acad. Sci. USA. 96:2627-2632.
17. Duprez, E., A.J. Saurin, J.M. Desterro, V. Lallemand-Breitenbach, K. Howe, M.N. Boddy, E. Solomon, H. de The, R.T. Hay, and P.S. Freemont. 1999. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J. Cell Sci. 112:381-393.
18. Dyck, J.A., G.G. Maul, W.H. Miller, Jr., J.D. Chen, A. Kakizuka, and R.M. Evans. 1994. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76:333-343.
19. Fagioli, M., M. Alcalay, L. Tomassoni, P.F. Ferrucci, A. Mencarelli, D. Riganelli, F. Grignani, T. Pozzan, I. Nicoletti, F. Grignani, and P.G. Pelicci. 1998. Cooperation between the RING + B1-B2 and coiled-coil domains of PML is necessary for its effects on cell survival. Oncogene. 16:2905-2913.
20. Fontes, J.D., S. Kanazawa, D. Jean, and B.M. Peterlin. 1999. Interactions between the class II transactivator and CREB binding protein increase transcription of major histocompatibility complex class 11 genes. Mol. Cell. Biol. 19:941-947.
21. Grande, M.A., I. van der Kraan, B. van Steensel, W. Schul, H. de The, H.T.M. van der Voort, L. de Jong, and R. van Driel. 1996. PML-containing nuclear bodies: their spatial distribution in relation to other nuclear components. J. Cell. Biochem. 63:280-291.
22. Grotzinger, T., T. Sternsdorf, K. Jensen, and H. Will. 1996. Interferon-modulated expression of genes encoding the nuclear-dot-associated proteins Sp100 and promyelocytic leukemia protein (PML). Eur. J. Biochem. 238: 554-560.
23. Guldner, H.H., C. Szostecki, T. Grotzinger, and H. Will. 1992. IFN enhance expression of Sp100, an autoantigen in primary biliary cirrhosis. J. Immunol. 149:4067-4073.
24. Hendzel, M.J., M.J. Kruhlak, and D.P. Bazett-Jones. 1998. Organization of highly acetylated chromatin around sites of heterogeneous nuclear RNA accumulation. Mol. Biol. Cell. 9:2491-2507.
25. Hendzel, M.J., F.-M. Boisvert, and D.P. Bazett-Jones. 1999. Direct visualization of a protein nuclear architecture. Mol. Biol. Cell. 10:2051-2062.
26. Ishov, A.M., and G.G. Maul. 1996. The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J Cell Biol. 134:815-826.
27. Ishov, A.M., R.M. Stenberg, and G.G. Maul. 1997. Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment. J. Cell Biol. 138:5-16.
28. Kakizuka, A., W.H. Miller, Jr., K. Umesono, R.P. Warrell, Jr., S.R. Frankel, V.V. Murty, E. Dmitrovsky, and R.M. Evans. 1991. Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell. 66:663-674.
29. Koken, M.H.M., F. Puvion-Dutilleul, M.C. Guillemin, A. Viron, G. Linares-Cruz., N. Stuurman, L. de Jong, C. Szostecki, F. Calvo, C. Chomienne, et al. 1994. The t(15;17) translocation alters a nuclear body in a retinoic acid-reversible fashion. EMBO (Eur. Mol. Biol. Organ.) J. 13:1073-1083.
30. Kretsovali, A., T. Agalioti, C. Spilianakis, E. Tzortzakaki, M. Merika, and J. Papamatheakis. 1998. Involvement of CREB binding protein in expression of major histocompatibility complex class 11 genes via interaction with the class II transactivator. Mol. Cell. Biol. 18:6777-6783.
31. LaMorte, V.J., J.A. Dyck, R.L. Ochs, and R.M. Evans. 1998. Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc. Natl. Acad Sci. USA. 95:4991-4996.
32. Lavau, C., A. Marchio, M. Fagioli, J. Jansen, B. Falini, P. Lebon, F. Grosveld. P.P. Pandolfi, P.G. Pelicci, and A. Dejean. 1995. The acute promyelocytic leukaemia-associated PML gene is induced by interferon. Oncogene. 11; 871-876.
33. Le, X.F., P. Yang, and K.S. Chang. 1996. Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML. J. Biol. Chem. 271:130-135.
34. Malatesta, M., C. Zancanaro, T.E. Martin, E.K. Chan, F. Amalric, R. Luhrmann, P. Vogel, and S. Fakan. 1994. Is the coiled body involved in nucleolar functions? Exp. Cell Res. 211:415-419.
35. Maul, G.G. 1998. Nuclear domain 10, the site of DNA virus transcription and replication. BioEssays. 20:660-667.
36. Maul, G.G., A.M. Ishov, and R.D. Everett. 1996. Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1. Virology. 217:67-75.
37. Muller, S., M.J. Matunis, and A. Dejean. 1998. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO (Eur. Mol. Biol. Organ.) J. 17:61-70.
38. Schul, W., L. de Jong, and R. van Driel. 1998. Nuclear neighbours: the spatial and functional organization of genes and nuclear domains. J. Cell Biochem. 70:159-171.
39. Slack, J.L., and R.E. Gallagher. 1999. The molecular biology of acute promyelocytic leukemia. Cancer Treat. Res. 99:75-124.
40. Smith, K.P., P.T. Moen, K.L. Wydner, J.R. Coleman, and J.B. Lawrence. 1999. Processing of endogenous pre-mRNAs in association with SC-35 domains is gene specific. J. Cell Biol. 144:617-629.
41. Sternsdorf, T., T. Grotzinger, K. Jensen, and H. Will. 1997a. Nuclear dots: actors on many stages. Immunobiol. 198:307-331.
42. Sternsdorf, T., K. Jensen, and H. Will. 1997b. Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by P1C1/ SUMO-1. J. Cell Biol. 139:1621-1634.
43. Sternsdorf, T., K. Jensen, B. Reich, and H. Will. 1999. The nuclear dot protein Sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol. Chem. 274:12555-12566.
44. Stuurman, N., A. de Graaf, A. Floore, A. Josso, B. Humbel, L. de Jong, and R. van Driel. 1992. A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies. J. Cell Sci. 101:773-784.
45. Szostecki, C., H.H. Guldner, H.J. Netter, and H. Will. 1990. Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J. Immunol. 145:4338-4347.
46. Vallian, S., J.A. Gaken, I.D. Trayner, E.B. Gingold, T. Kouzarides, K.S. Chang, and F. Farzaneh. 1997. Transcriptional repression by the promyelocytic leukemia protein, PML. Exp. Cell. Res. 237:371-382.
47. Vallian, S., K.V. Chin, and K.S. Chang. 1998a. The promyelocytic leukemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoter. Mol. Cell. Biol. 18:7147-7156.
48. Vallian, S., J.A. Gaken, E.B. Gingold, T. Kouzarides, K.S. Chang, and F. Farzaneh. 1998b. Modulation of Fos-mediated AP-1 transcription by the promyelocytic leukemia protein. Oncogene. 16:2843-2853.
49. Wang, Z.G., D. Ruggero, S. Ronchetti, S. Zhong, M. Gaboli, R. Rivi, and P.P. Pandolfi. 1998. PML is essential for multiple apoptotic pathways. Nat. Genet. 20:266-272.
50. Xie, K., E.J. Lambie, and M. Snyder. 1993. Nuclear dot antigens may specify transcriptional domains in the nucleus. Mol. Cell. Biol. 13:6170-6179.
51. Zheng, P., Y. Guo, Q. Niu, D.E. Levy, J.A. Dyck, S. Lu, L.A. Sheiman, and Y. Liu. 1998. Proto-oncogene PML controls genes devoted to MHC class I antigen presentation. Nature. 396:373-376.