Genomic structure, promoter activity, and developmental expression of the mouse homologue of the Machado-Joseph disease (MJD) gene

Genomics

Volumn 84, Issue 2, 2004, Pages 361-373

  Do Carmo Costa, Maria ^a,b   Gomes Da Silva, Joana ^a   Miranda, Carlos J ^a,c   Sequeiros, Jorge ^a,d   Santos, Manuela M ^a,c   Maciel, Patrícia ^a,b,d  

^a UNIVERSITY OF PORTO   (Portugal)

^b UNIVERSITY OF MINHO   (Portugal)

^c NOTRE DAME HOSPITAL   (Canada)

^d UNIVERSITY OF PORTO   (Portugal)

Author keywords

Arnt; Ataxin 3; E47; Max; Muscle; Myocytes; MyoD; Polyglutamine; Spinocerebellar ataxia; Triplet repeat

Indexed keywords

ATAXIN 3; MAX PROTEIN; MUTANT PROTEIN; MYOD PROTEIN; TATA BINDING PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ARNT; TRANSCRIPTION FACTOR E47; TRANSCRIPTION FACTOR SP1; UNCLASSIFIED DRUG; UPSTREAM STIMULATORY FACTOR;

5' UNTRANSLATED REGION; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BINDING SITE; CELL DIFFERENTIATION; CENTRAL NERVOUS SYSTEM; CONTROLLED STUDY; DEGENERATIVE DISEASE; DNA FLANKING REGION; EMBRYO; EMBRYO DEVELOPMENT; ENDODERM; GENE EXPRESSION; GENE STRUCTURE; HEART MUSCLE CELL; MACHADO JOSEPH DISEASE; MALE; MESODERM; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; SKELETAL MUSCLE; TERATOCARCINOMA;

5' FLANKING REGION; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CELL DIFFERENTIATION; CELL LINE; CLONING, MOLECULAR; DNA, COMPLEMENTARY; EMBRYO; GENE EXPRESSION REGULATION, DEVELOPMENTAL; MICE; MICE, INBRED C57BL; MYOD PROTEIN; NERVE TISSUE PROTEINS; NUCLEAR PROTEINS; PROMOTER REGIONS (GENETICS); PROTEIN BINDING; REPRESSOR PROTEINS; SEQUENCE ALIGNMENT; TRANSCRIPTION FACTORS;

ATAXIA;

EID: 3042604497     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ygeno.2004.02.012     Document Type: Article

References (46)

1. Margolis R.L. The spinocerebellar ataxias: order emerges from chaos. Curr. Neurol. Neurosci. Rep. 2:2002;447-456
2. Coutinho P., Andrade C. Autosomal dominant system degeneration in Portuguese families of the Azores Islands: a new genetic disorder involving cerebellar, pyramidal, extrapyramidal and spinal cord motor functions. Neurology. 28:1978;703-709
3. Rosenberg R.N. Machado-Joseph disease: an autosomal dominant motor system degeneration. Mov. Disord. 3:1992;193-203
4. Dürr A., et al. Spinocerebellar ataxia 3 and Machado-Joseph disease: clinical, molecular, and neuropathological features. Ann. Neurol. 39:1996;490-499
5. Takiyama Y., et al. The gene for the Machado-Joseph disease is mapped to human chromosome 14q. Nat. Genet. 4:1993;300-304
6. Kawaguchi Y., et al. CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1. Nat. Genet. 8:1994;221-228
7. Ichikawa Y., et al. The genomic structure and expression of MJD, the Machado-Joseph disease gene. J. Hum. Genet. 46:2001;413-422
8. Goto J., et al. Machado-Joseph disease gene products carrying different carboxyl termini. Neurosci. Res. 28:1997;373-377
9. Paulson H.L., et al. Machado-Joseph disease gene product is a cytoplasmic protein widely expressed in brain. Ann. Neurol. 41:1997;453-462
10. Trottier Y., et al. Heterogeneous intracellular localization and expression of ataxin-3. Neurobiol. Dis. 5:1998;335-347
11. Su A.I., et al. Large-scale analysis of the human and mouse transcriptomes. Proc. Natl. Acad. Sci. USA. 99:2002;4465-4470
12. Cummings C.J., Zoghbi H.Y. Fourteen and counting: unraveling trinucleotide repeat diseases. Hum. Mol. Genet. 9:2000;909-916
13. Maciel P., et al. Improvement in the molecular diagnosis of Machado-Joseph disease. Arch. Neurol. 58:2001;1821-1827
14. Schmidt T., et al. An isoform of ataxin-3 accumulates in the nucleus of neuronal cells in affected brain regions of SCA3 patients. Brain Pathol. 8:1998;669-679
15. Evert B.O., et al. High level expression of expanded full-length ataxin-3 in vitro causes cell death and formation of intranuclear inclusions in neuronal cells. Hum. Mol. Genet. 8:1999;1169-1176
16. Ikeda H., et al. Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo. Nat. Genet. 13:1996;196-202
17. Cemal C.K., et al. YAC transgenic mice carrying pathological alleles of the MJD1 locus exhibit a mild and slowly progressive cerebellar deficit. Hum. Mol. Genet. 11:2002;1075-1094
18. Ross C.A. Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron. 35:2002;819-822
19. Chan H.Y., Warrick J.M., Gray-Board G.L., Paulson H.L., Bonini N.M. Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila. Hum. Mol. Genet. 9:2000;2811-2820
20. Paulson H.L., Bonini N.M., Roth K.A. Polyglutamine disease and neuronal cell death. Proc. Natl. Acad. Sci. USA. 97:2000;12957-12958
21. Chai Y., Koppenhafer S.L., Shoesmith S.J., Perez M.K., Paulson H.L. Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum. Mol. Genet. 8:1999;673-682
22. Schmidt T., et al. Protein surveillance machinery in brains with spinocerebellar ataxia type 3: redistribution and differential recruitment of 26S proteasome subunits and chaperones to neuronal intranuclear inclusions. Ann. Neurol. 51:2002;302-310
23. Taylor J.P., Hardy J., Fischbeck K.H. Toxic proteins in neurodegenerative disease. Science. 296:2002;1991-1995
24. Bevivino A.E., Loll P.J. An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils. Proc. Natl. Acad. Sci. USA. 98:2001;11955-11960
25. Chen S., Berthelier V., Hamilton J.B., O'Nuallain B., Wetzel R. Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry. 41:2002;7391-7399
26. Wang G., Sawai N., Kotliarova S., Kanazawa I., Nukina N. Ataxin-3, the MJD1 product, interacts with two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. Hum. Mol. Genet. 9:2000;1795-1803
27. Li F., Macfarlan T., Pittman R.N., Chakravarti D. Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. J. Biol. Chem. 277:2002;45004-45012
28. Albrecht M., et al. Structural modeling of ataxin-3 reveals distant homology to adaptins. Proteins. 50:2003;355-370
29. Schmitt I., Brattig T., Gossen M., Riess O. Characterization of the rat spinocerebellar ataxia type 3 gene. Neurogenetics. 1:1997;103-112
30. Linhartova I., et al. Conserved domains and lack of evidence for polyglutamine length polymorphism in the chicken homolog of the Machado-Joseph disease gene product ataxin-3. Biochim. Biophys. Acta. 1444:1999;299-305
31. McBurney M.W., Jones-Villeneuve E.M., Edwards M.K., Anderson P.J. Control of muscle and neuronal differentiation in a cultured embryonal carcinoma cell line. Nature. 299:1982;165-167
32. Jones-Villeneuve E.M., McBurney M.W., Rogers K.A., Kalnis V.I. Retinoic acid induces embryonal carcinoma cells to differentiate into neurons and glial cells. J. Cell Biol. 94:1982;253-262
33. Banfi S., et al. Cloning and developmental expression analysis of the murine homolog of the spinocerebellar ataxia type 1 gene (Sca1). Hum. Mol. Genet. 5:1996;33-40
34. Nechiporuk T., et al. The mouse SCA2 gene: cDNA sequence, alternative splicing and protein expression. Hum. Mol. Genet. 7:1998;1301-1309
35. Strom A.L., et al. Cloning and expression analysis of the murine homolog of the spinocerebellar ataxia type 7 (SCA7) gene. Gene. 285:2002;91-99
36. Lin B., et al. Sequence of the murine Huntington disease gene: evidence for conservation, alternative splicing and polymorphism in a triplet (CCG) repeat. Hum. Mol. Genet. 3:1994;85-92
37. Barnes G.T., et al. Mouse Huntington's disease gene homolog (Hdh). Somatic Cell Mol. Genet. 20:1994;87-97
38. Skerjank I.S. Cardiac and skeletal muscle development in P19 embryonal carcinoma cells. Trends Cardiovasc. Med. 9:1999;139-143
39. Sarkar S.A., Sharma R.P. Modulation of c-myc, max, and mad gene expression during neural differentiation of embryonic stem cells by all-trans-retinoic acid. Gene Exp. 10:2002;125-135
40. Williams B.Y., Brommer S., Czarnetzki B.M., Rosenbach T. The differentiation-related upregulation of aryl hydrocarbon receptor transcript levels is suppressed by retinoic acid. Biochem. Biophys. Res. Commun. 209:1995;706-711
41. Altschul S.F., Gish W., Miller W., Myers E.W., Lipman D.J. Basic local alignment search tool. J. Mol. Biol. 215:1990;403-410
42. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680
43. Wingender E., et al. TRANSFAC: an integrated system for gene expression regulation. Nucleic Acids Res. 28:2000;316-319
44. J. Schug, G.C. Overton, TESS: Transcription Element Search Software on the WWW′, Technical Rep. CBIL-TR-1997-1001-v0.0, Computational Biology and Informatics Laboratory, School of Medicine, Univ. of Pennsylvania, Philadelphia, 1997.
45. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
46. Paxinos G., Franklin K.B.J. The Mouse Brain in Stereotaxic Coordinates. 1997;Academic Press, San Diego