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. 1987 Oct;84(19):6830–6834. doi: 10.1073/pnas.84.19.6830

Isolation and characterization of a cDNA clone for the Cat2 gene in maize and its homology with other catalases.

L A Bethards 1, R W Skadsen 1, J G Scandalios 1
PMCID: PMC299178  PMID: 2821546

Abstract

A 230-base-pair cDNA representing the 3' end of the Cat2 gene in maize was isolated and used to screen a lambda gt11 cDNA library made from scutellar poly(A)+ RNA. Several clones were subcloned into a pUC12 vector; one of the subclones, pCat2.1c, appears to represent a near-complete sequence of the Cat2 coding region. Immunological screening, hybridization-selection translation, and RNA blot analysis confirmed that pCat2.1c was derived from the Cat2 transcript. The DNA sequence of pCat2.1c was determined. The deduced amino acid sequence shows homology with catalase amino acid sequences from rat liver, bovine liver, human kidney, and yeast.

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Selected References

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

  1. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bailey J. M., Davidson N. Methylmercury as a reversible denaturing agent for agarose gel electrophoresis. Anal Biochem. 1976 Jan;70(1):75–85. doi: 10.1016/s0003-2697(76)80049-8. [DOI] [PubMed] [Google Scholar]
  3. Bell G. I., Najarian R. C., Mullenbach G. T., Hallewell R. A. cDNA sequence coding for human kidney catalase. Nucleic Acids Res. 1986 Jul 11;14(13):5561–5562. [PMC free article] [PubMed] [Google Scholar]
  4. Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [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. Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Gergen J. P., Stern R. H., Wensink P. C. Filter replicas and permanent collections of recombinant DNA plasmids. Nucleic Acids Res. 1979 Dec 20;7(8):2115–2136. doi: 10.1093/nar/7.8.2115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  10. Hall T. C., Ma Y., Buchbinder B. U., Pyne J. W., Sun S. M., Bliss F. A. Messenger RNA for G1 protein of French bean seeds: Cell-free translation and product characterization. Proc Natl Acad Sci U S A. 1978 Jul;75(7):3196–3200. doi: 10.1073/pnas.75.7.3196. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hartig A., Ruis H. Nucleotide sequence of the Saccharomyces cerevisiae CTT1 gene and deduced amino-acid sequence of yeast catalase T. Eur J Biochem. 1986 Nov 3;160(3):487–490. doi: 10.1111/j.1432-1033.1986.tb10065.x. [DOI] [PubMed] [Google Scholar]
  12. Kafatos F. C., Jones C. W., Efstratiadis A. Determination of nucleic acid sequence homologies and relative concentrations by a dot hybridization procedure. Nucleic Acids Res. 1979 Nov 24;7(6):1541–1552. doi: 10.1093/nar/7.6.1541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kopczynski C. C., Scandalios J. G. Cat-2 gene expression. Developmental control of translatable CAT-2 mRNA levels in maize scutellum. Mol Gen Genet. 1986 Apr;203(1):185–188. doi: 10.1007/BF00330401. [DOI] [PubMed] [Google Scholar]
  14. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  15. Mandel M., Higa A. Calcium-dependent bacteriophage DNA infection. J Mol Biol. 1970 Oct 14;53(1):159–162. doi: 10.1016/0022-2836(70)90051-3. [DOI] [PubMed] [Google Scholar]
  16. Michelson A. M., Orkin S. H. Characterization of the homopolymer tailing reaction catalyzed by terminal deoxynucleotidyl transferase. Implications for the cloning of cDNA. J Biol Chem. 1982 Dec 25;257(24):14773–14782. [PubMed] [Google Scholar]
  17. Miller J. S., Paterson B. M., Ricciardi R. P., Cohen L., Roberts B. E. Methods utilizing cell-free protein-synthesizing systems for the identification of recombinant DNA molecules. Methods Enzymol. 1983;101:650–674. doi: 10.1016/0076-6879(83)01046-0. [DOI] [PubMed] [Google Scholar]
  18. Murthy M. R., Reid T. J., 3rd, Sicignano A., Tanaka N., Rossmann M. G. Structure of beef liver catalase. J Mol Biol. 1981 Oct 25;152(2):465–499. doi: 10.1016/0022-2836(81)90254-0. [DOI] [PubMed] [Google Scholar]
  19. Norrander J., Kempe T., Messing J. Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene. 1983 Dec;26(1):101–106. doi: 10.1016/0378-1119(83)90040-9. [DOI] [PubMed] [Google Scholar]
  20. Palatnik C. M., Storti R. V., Jacobson A. Fractionation and functional analysis of newly synthesized and decaying messenger RNAs from vegetative cells of Dictyostelium discoideum. J Mol Biol. 1979 Mar 5;128(3):371–395. doi: 10.1016/0022-2836(79)90093-7. [DOI] [PubMed] [Google Scholar]
  21. Payvar F., Schimke R. T. Methylmercury hydroxide enhancement of translation and transcription of ovalbumin and conalbumin mRNA's. J Biol Chem. 1979 Aug 25;254(16):7636–7642. [PubMed] [Google Scholar]
  22. Quail P. H., Scandalios J. G. Turnover of genetically defined catalase isozymes in maize. Proc Natl Acad Sci U S A. 1971 Jul;68(7):1402–1406. doi: 10.1073/pnas.68.7.1402. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Scandalios J. G., Chang D. Y., McMillin D. E., Tsaftaris A., Moll R. H. Genetic regulation of the catalase developmental program in maize scutellum: Identification of a temporal regulatory gene. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5360–5364. doi: 10.1073/pnas.77.9.5360. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Scandalios J. G. Subunit dissociation and recombination of catalase isozymes. Proc Natl Acad Sci U S A. 1965 May;53(5):1035–1040. doi: 10.1073/pnas.53.5.1035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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]
  27. Skadsen R. W., Scandalios J. G. Evidence for processing of maize catalase 2 and purification of its messenger RNA aided by translation of antibody-bound polysomes. Biochemistry. 1986 Apr 22;25(8):2027–2032. doi: 10.1021/bi00356a029. [DOI] [PubMed] [Google Scholar]
  28. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  29. Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Tsaftaris A. S., Bosabalidis A. M., Scandalios J. G. Cell-type-specific gene expression and acatalasemic peroxisomes in a null Cat2 catalase mutant of maize. Proc Natl Acad Sci U S A. 1983 Jul;80(14):4455–4459. doi: 10.1073/pnas.80.14.4455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Vieira J., Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 1982 Oct;19(3):259–268. doi: 10.1016/0378-1119(82)90015-4. [DOI] [PubMed] [Google Scholar]
  32. Yamaguchi J., Nishimura M., Akazawa T. Maturation of catalase precursor proceeds to a different extent in glyoxysomes and leaf peroxisomes of pumpkin cotyledons. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4809–4813. doi: 10.1073/pnas.81.15.4809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Young R. A., Davis R. W. Efficient isolation of genes by using antibody probes. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1194–1198. doi: 10.1073/pnas.80.5.1194. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Young R. A., Davis R. W. Yeast RNA polymerase II genes: isolation with antibody probes. Science. 1983 Nov 18;222(4625):778–782. doi: 10.1126/science.6356359. [DOI] [PubMed] [Google Scholar]

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