The human cystathionine β-synthase (CBS) gene: Complete sequence, alternative splicing, and polymorphisms

Genomics

Volumn 52, Issue 3, 1998, Pages 312-324

  Kraus, Jan P ^a   Oliveriusová, Jana ^a,b   Sokolová, Jitka ^b   Kraus, Eva ^a   Vlček, Čestmír ^c   De Franchis, Raffaella ^a   Maclean, Kenneth N ^a   Bao, Liming ^a   Bukovská, Gabriela ^a   Patterson, David ^d   Pačes, Václav ^c   Ansorge, Wilhelm ^e   Kožich, Viktor ^b  

^a Children's Hospital Colorado   (United States)

^b Charles University in Prague and General University Hospital in Prague   (Czech Republic)

^c INSTITUTE OF MOLECULAR GENETICS   (Czech Republic)

^d UNIVERSITY OF DENVER   (United States)

^e EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTATHIONINE BETA SYNTHASE;

ALTERNATIVE RNA SPLICING; ARTICLE; ENZYME ANALYSIS; GENE LOCUS; GENE REARRANGEMENT; GENE SEQUENCE; GENETIC POLYMORPHISM; HOMOCYSTINURIA; HUMAN; HUMAN CELL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION;

EID: 0032531249     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.1998.5437     Document Type: Article

References (55)

1. Antonarakis, S. E. (1998). Recommendations for a nomenclature system for human gene mutations. Hum. Mutat. 11: 1-3.
2. Bao, L., Vlček, Č., Pačes, V., and Kraus, J. P. (1998). Identification and tissue distribution of human cystathionine beta-synthase messenger-RNA isoforms. Arch. Biochem. Biophys. 350: 95-103.
3. Barnes, W. M. (1994). PCR amplification of up to 35-kb DNA with high fidelity and high yield from lambda bacteriophage templates. Proc. Natl. Acad. Sci. USA 91: 2216-2220.
4. Bateman, A. (1997). The structure of a domain common to archae-bacteria and the homocystinuria protein. Trends Biochem. Sci. 22: 12-13.
5. Boers, G. H. J., Smals, A. G. H., Trijbels, F. J. M., Fowler, B., Bakkeren, J. A. J. M., Schoonderwaldt, H. C., Kleijer, W. J., and Kloppenborg, P. W. C. (1985). Heterozygosity for homocystinuria in premature peripheral and cerebral occlusive arterial disease. N. Engl. J. Med. 313: 709-715.
6. Boushey, C. J., Beresford, S. A. A., Omenn, G. S., and Motulsky, A. G. (1995). A quantitative assessment of plasma homocysteine as a risk factor for vascular disease. Probable benefits of increasing folic acid intakes. JAMA 274: 1049-1057.
7. Bukovská, G., Kery, V., and Kraus, J. P. (1994). Expression of human cystathionine β-synthase in Escherichia coli: Purification and characterization. Protein Expression Purif. 5: 442-448.
8. Chang, T. C., and Shapiro, D. J. (1990). An NF1-related vitellogenin activator element mediates transcription from the estrogen-regulated Xenopus laevis vitellogenin promoter. J. Biol. Chem. 265: 8176-8182.
9. Chassé, J. F., Paul, V., Escañez, R., Kamoun, P., and London, J. (1997). Human cystathionine β-synthase: Gene organization and expression of different 5′ alternative splicing. Mamm. Genome 8: 917-921.
10. Chomczynski, P., and Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159.
11. Clarke, R., Daly, L., Robinson, K., Naughten, E., Cahalane, S., Fowler, B., and Graham, I. (1991). Homocysteinemia: A risk factor for vascular disease. N. Engl. J. Med. 325: 967.
12. de Franchis, R., Kožich, V., McInnes, R. R., and Kraus, J. P. (1994). Identical genotypes in siblings with different homocystinuric phenotypes: Identification of three mutations in cystathionine β-synthase using an improved bacterial expression system. Hum. Mol. Genet. 3: 1103-1108.
13. Goldstein, J. L., Campbell, B. K., and Gartler, S. M. (1973). Homocystinuria: Heterozygote detection using phytohemagglutinin-stimulated lymphocytes. J. Clin. Invest. 52: 218-221.
14. Goss, S. J. (1984). Arginine synthesis by hepatomas in vitro. II. Isolation and characterization of Morris hepatoma variants unable to convert ornithine to arginine, and modulation of urea-cycle enzymes by dexamethasone and cyclic-AMP. J. Cell Sci. 68: 305-319.
15. Griffith, O. W. (1987). Mammalian sulfur amino acid metabolism: An overview. Methods Enzymol. 143: 366-376.
16. Jordan, M., Schallhorn, A., and Wurm, F. M. (1996). Transfecting mammalian cells: Optimization of critical parameters affecting calcium-phosphate precipitate formation. Nucleic Acids Res. 24: 596-601.
17. Jurka, J., Klonowski, P., Dagman, V., and Pelton, P. (1996). CENSOR - A program for identification and elimination of repetitive elements from DNA sequences. Comput. Chem. 20: 119-121.
18. Kaufman, P. B., Wu, W., and Cseke, L. J. (1995). "Handbook of Molecular and Cellular Methods in Biology and Medicine," CRC Press, Boca Raton, FL.
19. Kery, V., Bukovská, G., and Kraus, J. P. (1994). Transsulfuration depends on heme in addition to pyridoxal 5′-phosphate. Cystathionine β-synthase is a heme protein. J. Biol. Chem. 269: 25283-25288.
20. Kery, V., Poneleit, L., and Kraus, J.P. (1998a). Trypsin cleavage of human cystathionine β-synthase into an evolutionary conserved active core: Structural and functional consequences. Arch. Biochem. Biophys. 355: 222-232.
21. Kery, V., Poneleit, L., Meyer, J., Manning, M., and Kraus, J.P. (1998b). Binding of pyridoxal 5′-phosphate to a hemeprotein -human cystathionine β-synthase. FASEB J. 12: Abstr. 296.
22. Koiwai, O., Kaneda, T., and Morishita, R. (1987). Analysis of human terminal deoxynucleotidyl transferase cDNA expressible in mammalian cells. Biochem. Biophys. Res. Commun. 144: 185-190.
23. Korenberg, J. R., Kawashima, H., Pulst, S. M., Ikeuchi, T., Ogasawara, N., Yamamoto, K., Schonberg, S. A., West, R., Allen, L., Magenis, E., et al. (1990). Molecular definition of a region of chromosome 21 that causes features of the Down syndrome phenotype. Am. J. Hum. Genet. 47: 236-246.
24. Kožich, V., Kraus, E., de Franchis, R., Fowler, B., Boers, G. H. J., Graham, I., and Kraus, J. P. (1995). Hyperhomocysteinemia in premature arterial disease: Examination of cystathionine β-synthase alleles at the molecular level. Hum. Mol. Genet. 4: 623-629.
25. Kožich, V., and Kraus, J. P. (1992). Screening for mutations by expressing patient cDNA segments in E. coli - Homocystinuria due to cystathionine β-synthase deficiency. Hum. Mutat. 1: 113-123.
26. Kraus, J. P. (1994). Molecular basis of phenotype expression in homocystinuria. J. Inherited Metab. Dis. 17: 383-390.
27. Kraus, J.P. (1998). Biochemistry and molecular genetics of cystathionine β-synthase deficiency. Eur. J. Pediatr. 157(Suppl. 2): S50-S53.
28. Kraus, J. P., Le, K., Swaroop, M., Ohura, T., Tahara, T., Rosenberg, L. E., Roper, M. D., and Kožich, V. (1993). Human cystathionine β-synthase cDNA: Sequence, alternative splicing and expression in cultured cells. Hum. Mol. Genet. 2: 1633-1638.
29. Lehrman, M. A., Russell, D. W., Goldstein, J. L., and Brown, M. S. (1987). Alu-Alu recombination deletes splice acceptor sites and produces secreted low density lipoprotein receptor in a subject with familial hypercholesterolemia. J. Biol. Chem. 262: 3354-3361.
30. Long, M., Rosenberg, C., and Gilbert, W. (1995). Intron phase correlations and the evolution of the intron/exon structure of genes. Proc. Natl. Acad. Sci. USA 92: 12495-12499.
31. Markert, M. L., Hutton, J. J., Wiginton, D. A., States, J. C., and Kaufman, R. E. (1988). Adenosine deaminase (ADA) deficiency due to deletion of the ADA gene promoter and first exon by homologous recombination between two Alu elements. J. Clin. Invest. 81: 1323-1327.
32. Mudd, S. H., Levy, H. L., and Skovby, F. (1995). Disorders of transsulfuration. In "The Metabolic and Molecular Bases of Inherited Disease" (C. R. Scriver, A. L. Beaudet, W. S. Sly, and D. Valle, Eds.), pp. 1279-1327, McGraw-Hill, New York.
33. Munke, M., Kraus, J. P., Ohura, T., and Francke, U. (1988). The gene for cystathionine beta-synthase (CBS) maps to the subtelomeric region on human chromosome 21q and to proximal mouse chromosome 17. Am. J. Hum. Genet. 42: 550-559.
34. Nishio, Y., Isshiki, H., Kishimoto, T., and Akira, S. (1993). A nuclear factor for interleukin-6 expression (NF-IL6) and the glucocorticoid receptor synergistically activate transcription of the rat alpha 1-acid glycoprotein gene via direct protein-protein interaction. Mol. Cell. Biol. 13: 1854-1862.
35. Orendáč, M., Mušková, B., Richterová, F., Zvárová, J., Štefek, M.., Zayková, E., Stříbrný, J., Hyánek, J., Kraus, J.P., and Kožich, V. (1998). Mutation C677T in the MTHFR gene and polymorphism 844ins68 in the CBS gene: Risk factors for peripheral arterial occlusive disease ? Neth. J. Med. 52(Suppl.): S47.
36. Park, J. S., Luethy, J. D., Wang, M. G., Fargnoli, J., Fornace, A. J., Jr., McBride, O. W., and Holbrook, N. J. (1992). Isolation, characterization and chromosomal localization of the human GADD153 gene. Gene 116: 259-267.
37. Quandt, K., Frech, K., Karas, H., Wingender, E., and Werner, T. (1995). MatInd and MatInspector: New fast and versatile tools for detection of consensus matches in nucleotide sequence data. Nucleic Acids Res. 23: 4878-4884.
38. Roper, M. D., and Kraus, J. P. (1992). Rat cystathionine β-synthase: Expression of four alternatively spliced isoforms in transfected cultured cells. Arch. Biochem. Biophys. 298: 514-521.
39. Roper, M. D., Straubhaar, J. R., Kraus, E., Sokolová, J., Hřebíček, M., and Kraus, J. P. (1996). Comparison of the 5′ end of the rat and mouse cystathionine β-synthase genes. Mamm. Genome 7: 754-757.
40. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989). "Molecular Cloning: A Laboratory Manual," Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
41. Sebastio, G., Pia Sperandeo, M., Panico, M., de Franchis, R., Kraus, J., and Andria, G. (1995). The molecular basis of homocystinuria due to cystathionine β-synthase deficiency in Italian families, and report of four novel mutations. Am. J. Hum. Genet. 56: 1324-1333.
42. Selden, R. F., Howie, K B., Rowe, M. E., Goodman, H. M., and Moore, D. D. (1986). Human growth hormone as a reporter gene in regulation studies employing transient gene expression. Mol. Cell. Biol. 6: 3173-3179.
43. Selhub, J., and Miller, J. W. (1992). The pathogenesis of homocysteinemia: Interruption of the coordinate regulation by S-adenosyl-methionine of the remethylation and transsulfuration of homocysteine. Am. J. Clin. Nutr. 55: 131-138.
44. Shapiro, M. B., and Senapathy, P. (1987). RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression. Nucleic Acids Res. 15: 7155-7174.
45. Shepherd, N. S., Pfrogner, B. D., Coulby, J. N., Ackerman, S. L., Vaidyanathan, G., Sauer, R. H., Balkenhol, T. C., and Sternberg, N. (1994). Preparation and screening of an arrayed human genomic library generated with the Pl cloning system. Proc. Natl. Acad. Sci. USA 91: 2629-2633.
46. Soda, K. (1987). Microbial sulfur amino acids: An overview. Methods Enzymol. 143: 453-459.
47. Sperandeo, M. P., de Franchis, R., Andria, G., and Sebastio, G. (1996). A 68-bp insertion found in a homocystinuric patient is a common variant and is skipped by alternative splicing of the cystathionine β-synthase mRNA. Am. J. Hum. Genet. 59: 1391-1393.
48. Stoppa-Lyonnet, D., Carter, P. E., Meo, T., and Tosi, M. (1990). Clusters of intragenic Alu repeats predispose the human C1 inhibitor locus to deleterious rearrangements. Proc. Natl. Acad. Sci. USA 87: 1551-1555.
49. Swaroop, M., Bradley, K., Ohura, T., Tahara, T., Roper, M. D., Rosenberg, L. E., and Kraus, J. P. (1992). Rat cystathionine β-synthase. Gene organization and alternative splicing. J. Biol. Chem. 267: 11455-11461.
50. Tsai, M. Y., Bignell, M., Schwichtenberg, K., and Hanson, N. Q. (1996). High prevalence of a mutation in the cystathionine β-synthase gene. Am. J. Hum. Genet. 59: 1262-1267.
51. Tully, D. B., Allgood, V. E., and Cidlowski, J. A. (1994). Modulation of steroid receptor-mediated gene expression by vitamin B6 [review]. FASEB J. 8: 343-349.
52. van Santen, V. L., and Spritz, R. A. (1985). mRNA precursor splicing in vivo: Sequence requirements determined by deletion analysis of an intervening sequence. Proc. Natl. Acad. Sci. USA 82: 2885-2889.
53. Villena, J. A., Martin, I., Vinas, O., Cormand, B., Iglesias, R., Mampel, T., Giralt, M., and Villarroya, F. (1994). ETS transcription factors regulate the expression of the gene for the human mitochondrial ATP synthase beta-subunit. J. Biol. Chem. 269: 32649-32654.
54. Vlček, Č., and Pačes, V. (1995). A method for preparing M13 or pUC libraries for sequencing DNA with high G + C or A + T contents. Gene 165: 137-138.
55. Wingender, E., Kel, A. E., Kel, O. V., Karas, H., Heinemeyer, T., Dietze, P., Knuppel, R., Romaschenko, A. G., and Kolchanov, N. A. (1997). TRANSFAC, TRRD and COMPEL: Towards a federated database system on transcriptional regulation. Nucleic Acids Res. 25: 265-268.