Three extracellular proteases from Cochliobolus carbonum: Cloning and targeted disruption of ALP1

Molecular Plant-Microbe Interactions

Volumn 9, Issue 4, 1996, Pages 290-297

  Murphy, Jenifer M ^a   Walton, Jonathan D ^a  

^a MICHIGAN STATE UNIVERSITY   (United States)

Author keywords

Cell wall degrading enzyme; Helminthosporium; Maize; Trypsin; Virulence factor

Indexed keywords

COCHLIOBOLUS CARBONUM; FUNGI; HELMINTHOSPORIUM; HYPHOMYCETES; ZEA MAYS;

COMPLEMENTARY DNA; SERINE PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; ASCOMYCETES; ENZYMOLOGY; GENETIC TRANSFORMATION; GENETICS; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ASCOMYCOTA; BASE SEQUENCE; CLONING, MOLECULAR; DNA, COMPLEMENTARY; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; TRANSFORMATION, GENETIC;

EID: 0030136788     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI-9-0290     Document Type: Article

References (55)

1. Alexander, D., Lawton, K., Uknes, S., Ward, E., and Ryals, J. 1994. Defense-related gene induction in plants. Pages 195-212 in: Genetic Engineering, Vol. 16. J. K. Setlow, ed. Plenum Press, New York.
2. Ansari, H., and Stevens, L. 1983. Purification and properties of two neutral proteinases from Aspergillus nidulans. J. Gen. Microbiol. 129:1637-1644.
3. Apel, P. C., Panaccione, D. G., Holden, F. R., and Walton, J. D. 1993. Cloning and targeted gene disruption of XYLI, a β1,4-xylanase gene from the maize pathogen Cochliobolus carbonum. Mol. Plant-Microbe Interact. 6:467-473.
4. Ball, A. M., Ashby, A. M., Daniels, M. J., Ingram, D. S., and Johnstone, K. 1991. Evidence for the requirement of extracellular protease in the pathogenic interaction of Pyrenopeziza brassicae with oilseed rape. Physiol. Mol. Plant Pathol. 38:147-161.
5. Bateman, D. F., and Basham, H. G. 1976. Degradation of plant cell walls and membranes by microbial enzymes. Pages 316-355 in: Encyclopedia of Plant Physiology, New Series, Vol. 4. R. Heitefuss and P. H. Williams, eds. Springer-Verlag, New York.
6. Choi, G. H., Pawlyk, D. M., Rae, B., Shapira, R., and Nuss, D. L. 1993. Molecular analysis and overexpression of the gene encoding endothiapepsin, an aspartic protease from Cryphonectria parasitica. Gene 125:135-141.
7. Chomczynski, P., and Sacchi, N. 1987. Single step method of RNA extraction by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
8. Cooper, R. M. 1983. The mechanisms and significance of enzymic degradation of host cell walls by parasites. Pages 101-135 in: Biochemical Plant Pathology. J. A. Callow, ed. John Wiley & Sons, New York.
9. Dahler, G. S., Barras, F., and Keen, N. T. 1990. Cloning of genes encoding extracellular metalloproteases from Erwinia chrysanthemi EC16. J. Bacteriol. 172:5803-5815.
10. Devereux, J., Haeberli, P., and Smithies, O. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
11. Dow, J. M., Clarke, B. R., Milligan, D. E., Tang, J-L., and Daniels, M. J. 1990. Extracellular proteases from Xanthomonas campestris pv. campestris, the black rot pathogen. Appl. Environ. Microbiol. 56:2994-2998.
12. Drapeau, G. R. 1978. Role of a metalloprotease in activation of the precursor of Staphylococcal protease. J. Bacteriol. 136:607-613.
13. Edelmann, S. E., and Staben, C. 1994. A statistical analysis of sequence features within genes from Neurospora crassa. Exp. Mycol. 18:70-81.
14. Frohman, M. A., Dush, M. K., and Martin, G. R. 1988. Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA 85:8998-9002.
15. Gebhard, W., Tschesche, H., and Fritz, H. 1986. Biochemistry of aprotinin and aprotinin-like inhibitors. Pages 375-388 in: Proteinase Inhibitors. A. J. Barrett and G. Salvesen, eds. Elsevier Science, Amsterdam.
16. Gish, W., and States, D. J. 1993. Identification of protein coding regions by database similarity search. Nature Genet. 3:266-272.
17. Gurr, S. J., Unkles, S. E., and Kinghorn, J. R. 1987. The structure and organization of nuclear genes of filamentous fungi. Pages 93-139 in: Gene Structure in Eukaryotic Microbes. J. R. Kinghom, ed. IRL Press, London.
18. Hames, B. D., and Rickwood, D., eds. 1981. Gel Electrophoresis, A Practical Approach. IRL Press, Oxford.
19. Hislop, E. C., Paver, J. L., and Keon, J. P. R. 1982. An acid protease produced by Monilinia fructigena in vitro and in infected apple fruits, and its possible role in pathogenesis. J. Gen. Microbiol. 128:799-807.
20. Holden, F. R., and Walton, J. D. 1992. Xylanases from the fungal maize pathogen Cochliobolus carbonum. Physiol. Mol. Plant Pathol. 40:39-47.
21. Howard, S. P., and Buckley, J. T. 1985. Activation of the hole-forming toxin aerolysin by extracellular processing. J. Bacteriol. 163:336-340.
22. Ikeda, M., Yaginuma, T., Kobayashi, M., and Yamashita, O. 1991. cDNA cloning, sequencing and temporal expression of the protease responsible for vitellin degradation in the silkworm, Bombyx mon. Comp. Biochem. Physiol. 99B:405-411.
23. Lawton, M. A., and Lamb, C. J. 1987. Transcriptional activation of plant defense genes by fungal elicitor, wounding, and infection. Mol. Cell. Biol. 7:335-341.
24. Maniatis, T., Fritsch, E. F., and Sambrook, J. 1982. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
25. Matsudaira, P. 1987. Sequence from picomole quantitites of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:10035-10038.
26. McNeil, M., Darvill, A. G., Fry, S. C., and Albersheim, P. 1984. Structure and function of the primary cell walls of plants. Annu. Rev. Biochem. 53:625-663.
27. Monod, M., Paris, S., Sarfati, J., Jaton-Ogay, K., Ave, P., and Latgé, J.-P. 1993. Virulence of alkaline protease-deficient mutants of Aspergillus fumigatus. FEMS Microbiol. Lett. 106:39-46.
28. Moormann, M., Schlochtermeier, A., and Schrempf, H. 1993. Biochemical characterization of a protease involved in the processing of a Streptomyces reticuli cellulase (Avicelase). Appl. Environ. Microbiol. 59:1573-1578.
29. Murphy, J. M., and Hood, E. E. 1993. Molecular basis for extensin size heterogeneity in two maize varieties. Plant Mol. Biol. 21:885-893.
30. Neurath, H. 1984. Evolution of proteolytic enzymes. Science 224:350-357.
31. North, M. J. 1982. Comparative biochemistry of the proteinases of eukaryotic microorganisms. Microbiol. Rev. 46:308-340.
32. Olafson, R. W., Jurasek, L., Carpenter, M. R., and Smillie, L. B. 1975. Amino acid sequence of Streptomyces griseus trypsin. Cyanogen bromide fragments and complete sequence. Biochemistry 14:1168-1177.
33. Ottensen, M., and Svendsen, I. 1970. The subtilisins. Pages 199-215 in: Methods in Enzymotogy: Proteolytic Enzymes, Vol. 19. G. E. Perlmann and L. Lorand, eds. Academic Press, Orlando.
34. Pitkin, J. W., Panaccione, D. G., and Walton, J. D. 1996. A putative cyclic peptide efflux pump encoded by the TOXA gene of the plant pathogenic fungus Cochliobolus carbonum. Microbiology, in press.
35. Porter, F. M. 1966. Protease activity in diseased fruits. Phytopathology 56:1424-1425.
36. Powers, J. C., and Harper, E. A. 1986. Inhibitors of serine proteases. Pages 55-152 in: Protease Inhibitors, A. J. Barrett and G. Salvesen, eds. Elsevier Science, Amsterdam.
37. Reddy, M. N., Stuteville, D. L., and Sorensen, E. L. 1971. Protease production during pathogenesis of bacterial leaf spot of alfalfa and by Xanthomonas alfalfae in vitro. Phytopathology 61:361-365.
38. Ries, S. M., and Albersheim, P. 1973. Purification of a protease secreted by Colletotrichum lindemuthianum. Phytopathology 63:625-629.
39. Robertsen, B. 1984. An alkaline protease produced by Cladosporium cucumerinum and its possible importance in the development of scab disease of cucumber seedlings. Physiol. Plant Pathol. 24:83-92.
40. Ryan, C. A. 1990. Protease inhibitors in plants: Genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 28:425-429.
41. Rypniewski, W. R., Hastrup, S., Betzel, C., Dauter, M., Dauter, Z., Papendorf, G., Branner, S., and Wilson, K. S. 1993. The sequence and X-ray structure of the trypsin from Fusarium oxysporum. Protein Engineer. 6:341-348.
42. Schäfer, W., Straney, D., Cuiffetti, L., Van Etten, H. D., and Yoder, O. C. 1989. One enzyme makes a fungal pathogen, but not a saprophyte, virulent on a new host plant. Science 246:247-249.
43. Scott-Craig, J. S., Panaccione, D. G., Cervone, F., and Walton, J. D. 1990. Endopolygalacturonase is not required for pathogenicity of Cochliobolus carbonum on maize. Plant Cell 2:1191-1200.
44. Showalter, A. M. 1993. Structure and function of plant cell wall proteins. Plant Cell 5:9-23.
45. Sposato, P., Ahn, J.-H., and Walton, J. D. 1995. Characterization and disruption of a gene in the maize pathogen Cochliobolus carbonum encoding a cellulase lacking a cellulose binding domain and hinge region. Mol. Plant-Microbe Interact. 8:602-609.
46. Strömqvist, M., and Gruffman, H. 1992. Periodic acid/Schiff staining of glycoproteins immobilized on a blotting matrix. BioTechniques 13:744-746.
47. Tang, C. M., Cohen, J., Krausz, T., Van Noorden, S., and Holden, D. W. 1993. The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis. Infect. Immun. 61:1650-1656.
48. Tseng, T. C., and Mount, M. S. 1974. Toxicity of endopolygalacturonate trans-eliminase, phosphatidase, and protease to potato and cucumber tissue. Phytopathology 64:229-236.
49. van den Ackerveken, G. F. J. M., Vossen, P., and De Wit, P. J. G. M. 1993. The AVR9 race-specific elicitor of Cladosporium fulvum is processed by endogenous and plant proteases. Plant Physiol. 103:91-96.
50. van Hoof, A., Leykam, J., Schaeffer, H. J., and Walton, J. D. 1991. A single β1,3-glucanase secreted by the maize pathogen Cochliobolus carbonum acts by an exolytic mechanism. Physiol. Mol. Plant Pathol. 39:259-267.
51. von Heijne, G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683-4690.
52. Walsh, K. A., and Neurath, H. 1964. Trypsinogen and chymotrypsinogen as homologous proteins. Proc. Natl. Acad. Sci. USA 52:884-889.
53. Walsh, K. A., and Wilcox, P. E. 1970. Serine proteases. Pages 31-63 in: Methods in Enzymology: Proteolytic Enzymes, Vol. 19. G. E. Perlmann and L. Lornad, eds. Academic Press, Orlando.
54. Walton, J. D. 1994. Deconstructing the cell wall. Plant Physiol. 104:1113-1118.
55. Walton, J. D., and Cervone, F. 1990. Endopolygalacturonase from the maize pathogen Cochliobolus carbonum. Physiol. Mol. Plant Pathol. 36:351-359.