1887

Abstract

Two new cellulose-growth specific () cDNAs, and , have been isolated from an cDNA expression library by immunoscreening with an anti-endoglucanase antibody. The deduced amino acid sequences showed that both CEL2 and CEL4 proteins have a modular structure consisting of a fungal-type cellulose-binding domain (CBD) and a catalytic domain separated by a linker region rich in Pro, Ser and Thr. The CEL2 and CEL4 catalytic domains were homologous to fungal cellobiohydrolases (CBH) in family 7 and to fungal mannanases in family 5 of the glycosyl hydrolases, respectively. A previously isolated cDNA derived from a constitutive gene was also sequenced. The deduced amino acid sequence corresponded to 5-aminolaevulinic acid synthase (ALA), the first enzyme in the haem biosynthetic pathway, and was most similar to other fungal ALAs. RNA analysis showed that the expression of and genes was induced by cellulose and repressed by glucose, fructose and lactose. The soluble cellulose derivative CM-cellulose induced mRNA accumulation for but not or Mannitol, maltose, sorbitol and glycerol decreased and mRNA levels to different extents, and mRNAs all disappeared after the addition of glucose with apparent half-lives of less than 20 min. Whether mRNAs have short half-lives or glucose affects the stability of transcripts remains to be investigated.

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1997-01-01
2021-05-15
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References

  1. Aho S., Paloheimo M. 1990; The conserved terminal region of Trichoderma reesei cellulases forms a strong antigenic epitope for polyclonal antibodies.. Biochim Biophys Acta 1087:137–141
    [Google Scholar]
  2. Arisan-Atac I., Hodits R., Kristufek D., Kubicek C.P. 1993; Purification and characterization of a β-mannanase of Tricho- derma reesei C-30.. Appl Environ Microbiol 39:58–62
    [Google Scholar]
  3. Armesilla A.L., Thurston C.F., Yagüe E. 1994; CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.. FEMS Microbiol Lett 116:293–300
    [Google Scholar]
  4. Béguin P., Aubert J.-P. 1994; The biological degradation of cellulose.. FEMS Microbiol Rev 13:25–58
    [Google Scholar]
  5. Bradshaw R.E., Dixon S.W.C., Raitt D.C., Pillar T.M. 1993; Isolation and nucleotide sequence of the 5-aminolevulinate synthase gene from Aspergillus nidulans. . Curr Genet 23:501–507
    [Google Scholar]
  6. Chow C.-M., Yagüe E., Raguz S., Wood D.A., Thurston C.F. 1994; The cel3 gene of Agaricus bisporus codes for a modular cellulase and is transcriptionally regulated by the carbon source.. Appl Environ Microbiol 60:2779–2785
    [Google Scholar]
  7. Conboy J.G., Cox T.C., Bottomley S.S., Bawden M.J., May B.K. 1992; Human erythroid 5-aminolevulinate synthase. Gene structure and species-specific differences in alternative RNA splicing.. J Biol Chem 267:18753–18758
    [Google Scholar]
  8. Divne C., Ståhlberg J., Reinikainen T., Ruohonen L., Pettersson G., Knowles J.K.C., Teeri T.T., Jones T.A. 1994; The threedimensional crystal structure of the catalytic core of cellobio- hydrolase I from Trichoderma reesei. . Science 265:524–528
    [Google Scholar]
  9. Federoff H.J., Eccleshall T.R., Marmur J. 1983; Carbon catabolite repression of maltase synthesis in Saccharomyces carlsbergensis. . J Bacteriol 156:301–307
    [Google Scholar]
  10. 1991 Program Manual for the GCG Package, Version 7. GCG: 575 Science Drive; Madison, WI 53711, USA.:
    [Google Scholar]
  11. Henrissat B. 1991; A classification of glycosyl hydrolases based on amino acid sequence similarities.. Biochem J 280:309–316
    [Google Scholar]
  12. Henrissat B., Bairoch A. 1993; New families in the classification of glycosyl hydrolases based on amino acid sequence similarities.. Biochem J 293:781–788
    [Google Scholar]
  13. Keng T., Guarente L. 1987; Constitutive expression of the yeast HEM1 gene is actually a composite of activation and repression.. Proc Natl Acad Sci USA 849113–9117
    [Google Scholar]
  14. Lombardo A., Cereghino G.P., Scheffler I.E. 1992; Control of mRNA turnover as a mechanism of glucose repression in Saccharomyces cerevisiae. . Mol Cell Biol 12:2941–2948
    [Google Scholar]
  15. Manning K., Wood D.A. 1983; Production and regulation of extracellular endocellulase by Agaricus bisporus. . J Gen Microbiol 129:1839–1847
    [Google Scholar]
  16. Melefors O., Goossen B., Johansson H.E., Stripecke R., Gray N.K., Hentze M.W. 1993; Translational control of 5- aminolevulinate synthase mRNA by iron-responsive elements in erythroid cells.. J Biol Chem 268:5974–5978
    [Google Scholar]
  17. Ooi T., Shinmyo A., Okada H., Murao S., Kawaguchi T., Arai M. 1990; Complete nucleotide sequence of a gene coding for Aspergillus aculeatus cellulase (Fl-CMCase).. Nucleic Acids Res 18:5884
    [Google Scholar]
  18. Parker R., Herrick D., Peltz S.W., Jacobson A. 1991; Measurement of mRNA decay rates in Saccharomyces cerevisiae. . Methods Enzymol 194:415–423
    [Google Scholar]
  19. Raguz S., Yagüe E., Wood D.A., Thurston C.F. 1992; Isolation and characterization of a cellulose-growth-specific gene from Agaricus bisporus. . Gene 119:183–190
    [Google Scholar]
  20. Rouvinen J., Bergfords T., Teeri T., Knowles J.K.C., Jones T.A. 1990; Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. . Science 249:380–386
    [Google Scholar]
  21. Stålbrand H., Siika-aho M., Tenkanen M., Viikari L. 1993; Purification and characterization of two β-mannanases from Trichoderma reesei. . J Biotechnol 29:229–242
    [Google Scholar]
  22. Stålbrand H., Saloheimo A., Vehmaanperä J., Henrissat B., Penttilä M. 1995; Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei β-mannanase gene containing a cellulose binding domain.. Appl Environ Microbiol 61:1090–1097
    [Google Scholar]
  23. Wood D.A., Thurston C.F. 1991; Progress in the molecular analysis of Agaricus enzymes.. In Genetics and Breeding of Agaricus pp. 81–86 Van Griensven L. J. L. D. Edited by Wageningen:: Pudoc.;
    [Google Scholar]
  24. Wood D.A., Claydon N., Dudley K.J., Stephens S.K., Allan M. 1988; Cellulase production in the life cycle of the cultivated mushroom Agaricus bisporus. . In Biochemistry and Genetics of Cellulose Degradation pp. 53–70 Aubert J.-P., Béguin P., Millet J. Edited by London:: Academic Press.;
    [Google Scholar]
  25. Yagüe E., Béguin P., Aubert J.-P. 1990; Nucleotide sequence and deletion analysis of the cellulase-encoding gene celH of Clostridium thermocellum. . Gene 89:61–67
    [Google Scholar]
  26. Yagüe E., Wood D.A., Thurston C.F. 1994; Regulation of transcription of the cell gene in Agaricus bisporus. . Mol Microbiol 12:41–47
    [Google Scholar]
  27. Yagüe E., Chow C.-M., Challen M.P., Thurston C.F. 1996; Correlation of exons with functional domains and folding regions in a cellulase from Agaricus bisporus. . Curr Genet 30:56–61
    [Google Scholar]
  28. Yamamoto M., Kure S., Engel J.D., Hiraga K. 1988; Structure, turnover, and heme-mediated suppression of the level of mRNA encoding rat liver delta-aminolevulinate synthase.. J Biol Chem 263:15973–15979
    [Google Scholar]
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