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. 1986 Jul 11;14(13):5321–5335. doi: 10.1093/nar/14.13.5321

Isolation and characterization of the human catalase gene.

F Quan, R G Korneluk, M B Tropak, R A Gravel
PMCID: PMC311543  PMID: 3755525

Abstract

Catalase is a tetrameric hemoprotein which degrades H2O2. Recombinant phage clones containing the human catalase gene have been isolated and characterized. The gene is 34 kb long and is split into 13 exons. The precise size and location of the exons has been determined. In addition, essentially full length catalase cDNA clones have been isolated and sequenced and used to tentatively identify the 5'-end of the gene. This assignment, if correct, predicts that the region upstream of the gene does not contain a TATA box. This region is GC rich (67%) and contains several CCAAT and GGGCGG sequences which may form part of the promoter. Translation of the catalase mRNA appears to begin immediately upstream of the amino-terminal Ala residue of catalase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Benoist C., O'Hare K., Breathnach R., Chambon P. The ovalbumin gene-sequence of putative control regions. Nucleic Acids Res. 1980 Jan 11;8(1):127–142. doi: 10.1093/nar/8.1.127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Birnstiel M. L., Busslinger M., Strub K. Transcription termination and 3' processing: the end is in site! Cell. 1985 Jun;41(2):349–359. doi: 10.1016/s0092-8674(85)80007-6. [DOI] [PubMed] [Google Scholar]
  3. Breathnach R., Chambon P. Organization and expression of eucaryotic split genes coding for proteins. Annu Rev Biochem. 1981;50:349–383. doi: 10.1146/annurev.bi.50.070181.002025. [DOI] [PubMed] [Google Scholar]
  4. Cech T. R. RNA splicing: three themes with variations. Cell. 1983 Oct;34(3):713–716. doi: 10.1016/0092-8674(83)90527-5. [DOI] [PubMed] [Google Scholar]
  5. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  6. Deisseroth A., Dounce A. L. Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role. Physiol Rev. 1970 Jul;50(3):319–375. doi: 10.1152/physrev.1970.50.3.319. [DOI] [PubMed] [Google Scholar]
  7. Dynan W. S., Sazer S., Tjian R., Schimke R. T. Transcription factor Sp1 recognizes a DNA sequence in the mouse dihydrofolate reductase promoter. Nature. 1986 Jan 16;319(6050):246–248. doi: 10.1038/319246a0. [DOI] [PubMed] [Google Scholar]
  8. Dynan W. S., Tjian R. Control of eukaryotic messenger RNA synthesis by sequence-specific DNA-binding proteins. 1985 Aug 29-Sep 4Nature. 316(6031):774–778. doi: 10.1038/316774a0. [DOI] [PubMed] [Google Scholar]
  9. Dynan W. S., Tjian R. Isolation of transcription factors that discriminate between different promoters recognized by RNA polymerase II. Cell. 1983 Mar;32(3):669–680. doi: 10.1016/0092-8674(83)90053-3. [DOI] [PubMed] [Google Scholar]
  10. Dynan W. S., Tjian R. The promoter-specific transcription factor Sp1 binds to upstream sequences in the SV40 early promoter. Cell. 1983 Nov;35(1):79–87. doi: 10.1016/0092-8674(83)90210-6. [DOI] [PubMed] [Google Scholar]
  11. Everett R. D., Baty D., Chambon P. The repeated GC-rich motifs upstream from the TATA box are important elements of the SV40 early promoter. Nucleic Acids Res. 1983 Apr 25;11(8):2447–2464. doi: 10.1093/nar/11.8.2447. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Frischauf A. M., Garoff H., Lehrach H. A subcloning strategy for DNA sequence analysis. Nucleic Acids Res. 1980 Dec 11;8(23):5541–5549. doi: 10.1093/nar/8.23.5541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Fujiki Y., Rachubinski R. A., Mortensen R. M., Lazarow P. B. Synthesis of 3-ketoacyl-CoA thiolase of rat liver peroxisomes on free polyribosomes as a larger precursor. Induction of thiolase mRNA activity by clofibrate. Biochem J. 1985 Mar 15;226(3):697–704. doi: 10.1042/bj2260697. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Furuta S., Hashimoto T., Miura S., Mori M., Tatibana M. Cell-free synthesis of the enzymes of peroxisomal beta-oxidation. Biochem Biophys Res Commun. 1982 Mar 30;105(2):639–646. doi: 10.1016/0006-291x(82)91482-6. [DOI] [PubMed] [Google Scholar]
  15. Furuta S., Hayashi H., Hijikata M., Miyazawa S., Osumi T., Hashimoto T. Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase. Proc Natl Acad Sci U S A. 1986 Jan;83(2):313–317. doi: 10.1073/pnas.83.2.313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Gidoni D., Dynan W. S., Tjian R. Multiple specific contacts between a mammalian transcription factor and its cognate promoters. 1984 Nov 29-Dec 5Nature. 312(5993):409–413. doi: 10.1038/312409a0. [DOI] [PubMed] [Google Scholar]
  17. Guo L. H., Yang R. C., Wu R. An improved strategy for rapid direct sequencing of both strands of long DNA molecules cloned in a plasmid. Nucleic Acids Res. 1983 Aug 25;11(16):5521–5540. doi: 10.1093/nar/11.16.5521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Hartzell S. W., Byrne B. J., Subramanian K. N. Mapping of the late promoter of simian virus 40. Proc Natl Acad Sci U S A. 1984 Jan;81(1):23–27. doi: 10.1073/pnas.81.1.23. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Jones K. A., Tjian R. Sp1 binds to promoter sequences and activates herpes simplex virus 'immediate-early' gene transcription in vitro. Nature. 1985 Sep 12;317(6033):179–182. doi: 10.1038/317179a0. [DOI] [PubMed] [Google Scholar]
  20. Junien C., Turleau C., Lenoir G. M., Philip T., Said R., Despoisse S., Laurent C., Rethoré M. O., Kaplan J. C., de Grouchy J. Catalase determination in various etiologic forms of Wilms' tumor and gonadoblastoma. Cancer Genet Cytogenet. 1983 Sep;10(1):51–57. doi: 10.1016/0165-4608(83)90105-x. [DOI] [PubMed] [Google Scholar]
  21. Junien C., Turleau C., de Grouchy J., Saïd R., Rethoré MO L., Tenconi R., Dufier J. L. Regional assignment of catalase (CAT) gene to band 11p13. Association with the aniridia-Wilms' tumor-Gonadoblastoma (WAGR) complex. Ann Genet. 1980;23(3):165–168. [PubMed] [Google Scholar]
  22. Korneluk R. G., Quan F., Gravel R. A. Rapid and reliable dideoxy sequencing of double-stranded DNA. Gene. 1985;40(2-3):317–323. doi: 10.1016/0378-1119(85)90055-1. [DOI] [PubMed] [Google Scholar]
  23. Korneluk R. G., Quan F., Lewis W. H., Guise K. S., Willard H. F., Holmes M. T., Gravel R. A. Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA. J Biol Chem. 1984 Nov 25;259(22):13819–13823. [PubMed] [Google Scholar]
  24. Kozak M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 1984 Jan 25;12(2):857–872. doi: 10.1093/nar/12.2.857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Kwok S. C., Ledley F. D., DiLella A. G., Robson K. J., Woo S. L. Nucleotide sequence of a full-length complementary DNA clone and amino acid sequence of human phenylalanine hydroxylase. Biochemistry. 1985 Jan 29;24(3):556–561. doi: 10.1021/bi00324a002. [DOI] [PubMed] [Google Scholar]
  26. Lawn R. M., Fritsch E. F., Parker R. C., Blake G., Maniatis T. The isolation and characterization of linked delta- and beta-globin genes from a cloned library of human DNA. Cell. 1978 Dec;15(4):1157–1174. doi: 10.1016/0092-8674(78)90043-0. [DOI] [PubMed] [Google Scholar]
  27. McKnight S. L., Kingsbury R. Transcriptional control signals of a eukaryotic protein-coding gene. Science. 1982 Jul 23;217(4557):316–324. doi: 10.1126/science.6283634. [DOI] [PubMed] [Google Scholar]
  28. McLauchlan J., Gaffney D., Whitton J. L., Clements J. B. The consensus sequence YGTGTTYY located downstream from the AATAAA signal is required for efficient formation of mRNA 3' termini. Nucleic Acids Res. 1985 Feb 25;13(4):1347–1368. doi: 10.1093/nar/13.4.1347. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Melton D. A., Krieg P. A., Rebagliati M. R., Maniatis T., Zinn K., Green M. R. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 1984 Sep 25;12(18):7035–7056. doi: 10.1093/nar/12.18.7035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Melton D. W., Konecki D. S., Brennand J., Caskey C. T. Structure, expression, and mutation of the hypoxanthine phosphoribosyltransferase gene. Proc Natl Acad Sci U S A. 1984 Apr;81(7):2147–2151. doi: 10.1073/pnas.81.7.2147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Miura S., Mori M., Takiguchi M., Tatibana M., Furuta S., Miyazawa S., Hashimoto T. Biosynthesis and intracellular transport of enzymes of peroxisomal beta-oxidation. J Biol Chem. 1984 May 25;259(10):6397–6402. [PubMed] [Google Scholar]
  32. Ogata M., Mizugaki J. Properties of residual catalase in the erythrocytes of Japanese-type acatalasemia. Hum Genet. 1979 May 10;48(3):329–338. doi: 10.1007/BF00272833. [DOI] [PubMed] [Google Scholar]
  33. Proudfoot N. J., Brownlee G. G. 3' non-coding region sequences in eukaryotic messenger RNA. Nature. 1976 Sep 16;263(5574):211–214. doi: 10.1038/263211a0. [DOI] [PubMed] [Google Scholar]
  34. Quan F., Korneluk R. G., MacLeod H. L., Tsui L. C., Gravel R. A. An RFLP associated with the human catalase gene. Nucleic Acids Res. 1985 Nov 25;13(22):8288–8288. doi: 10.1093/nar/13.22.8288. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Rachubinski R. A., Fujiki Y., Mortensen R. M., Lazarow P. B. Acyl-Coa oxidase and hydratase-dehydrogenase, two enzymes of the peroxisomal beta-oxidation system, are synthesized on free polysomes of clofibrate-treated rat liver. J Cell Biol. 1984 Dec;99(6):2241–2246. doi: 10.1083/jcb.99.6.2241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Reynolds G. A., Basu S. K., Osborne T. F., Chin D. J., Gil G., Brown M. S., Goldstein J. L., Luskey K. L. HMG CoA reductase: a negatively regulated gene with unusual promoter and 5' untranslated regions. Cell. 1984 Aug;38(1):275–285. doi: 10.1016/0092-8674(84)90549-x. [DOI] [PubMed] [Google Scholar]
  37. Robbi M., Lazarow P. B. Peptide mapping of peroxisomal catalase and its precursor. Comparison to the primary wheat germ translation product. J Biol Chem. 1982 Jan 25;257(2):964–970. [PubMed] [Google Scholar]
  38. Robbi M., Lazarow P. B. Synthesis of catalase in two cell-free protein-synthesizing systems and in rat liver. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4344–4348. doi: 10.1073/pnas.75.9.4344. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Schroeder W. A., Shelton J. R., Shelton J. B., Apell G., Evans L., Bonaventura J., Fang R. S. The partial amino acid sequence of human erythrocyte catalase. Arch Biochem Biophys. 1982 Mar;214(1):422–424. doi: 10.1016/0003-9861(82)90045-5. [DOI] [PubMed] [Google Scholar]
  41. Schroeder W. A., Shelton J. R., Shelton J. B., Robberson B., Apell G., Fang R. S., Bonaventura J. The complete amino acid sequence of bovine liver catalase and the partial sequence of bovine erythrocyte catalase. Arch Biochem Biophys. 1982 Mar;214(1):397–421. doi: 10.1016/0003-9861(82)90044-3. [DOI] [PubMed] [Google Scholar]
  42. Shingu M., Yoshioka K., Nobunaga M., Yoshida K. Human vascular smooth muscle cells and endothelial cells lack catalase activity and are susceptible to hydrogen peroxide. Inflammation. 1985 Sep;9(3):309–320. doi: 10.1007/BF00916279. [DOI] [PubMed] [Google Scholar]
  43. Valerio D., Duyvesteyn M. G., Dekker B. M., Weeda G., Berkvens T. M., van der Voorn L., van Ormondt H., van der Eb A. J. Adenosine deaminase: characterization and expression of a gene with a remarkable promoter. EMBO J. 1985 Feb;4(2):437–443. doi: 10.1002/j.1460-2075.1985.tb03648.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Wieacker P., Mueller C. R., Mayerova A., Grzeschik K. H., Ropers H. H. Assignment of the gene coding for human catalase to the short arm of chromosome 11. Ann Genet. 1980;23(2):73–77. [PubMed] [Google Scholar]
  45. Willard H. F., Smith K. D., Sutherland J. Isolation and characterization of a major tandem repeat family from the human X chromosome. Nucleic Acids Res. 1983 Apr 11;11(7):2017–2033. doi: 10.1093/nar/11.7.2017. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. van Heyningen V., Boyd P. A., Seawright A., Fletcher J. M., Fantes J. A., Buckton K. E., Spowart G., Porteous D. J., Hill R. E., Newton M. S. Molecular analysis of chromosome 11 deletions in aniridia-Wilms tumor syndrome. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8592–8596. doi: 10.1073/pnas.82.24.8592. [DOI] [PMC free article] [PubMed] [Google Scholar]

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