A distinct member of the basic (class I) chitinase gene family in potato is specifically expressed in epidermal cells

Plant Molecular Biology

Volumn 39, Issue 6, 1999, Pages 1137-1151

  Ancillo, Gema ^a,b   Witte, Bärbel ^a,c   Schmelzer, Elmon ^a   Kombrink, Erich ^a  

^a MAX PLANCK INSTITUTE FOR PLANT BREEDING RESEARCH   (Germany)

^b Universitat Politècnica de València   (Spain)

^c Focus AFA   (Germany)

Author keywords

Fungal elicitor; Infection; Pathogenesis related protein; Phytophthora infestans; Plant defense; Wounding

Indexed keywords

AMINO ACID SEQUENCE; CHITINASE GENE; EPIDERMIS CELL; GENE EXPRESSION; IN SITU HYBRIDIZATION; NUCLEOTIDE SEQUENCE; POTATO;

ANIMALIA; EMBRYOPHYTA; FUNGI; PHYTOPHTHORA INFESTANS; SOLANUM TUBEROSUM;

EID: 0033121062     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006178425803     Document Type: Article

References (52)

1. Abeles FB, Bosshart RP, Forrence LE, Habig WH: Preparation and purification of glucanase and chitinase from bean leaves. Plant Physiol 47: 129-134 (1971).
2. Bartnicki-Garcia S: Cell wall chemistry, morphogenesis, and taxonomy of fungi. Annu Rev Microbiol 22: 87-108 (1968).
3. Beerhues L, Kombrink E: Primary structure and expression of mRNAs encoding basic chitinase and 1,3-β-glucanase in potato. Plant Mol Biol 24: 353-367 (1994).
4. Boller T: Ethylene and the regulation of antifungal hydrolases in plants. In: Miflin BJ (ed) Oxford Surveys of Plant Molecular and Cell Biology, vol 5, pp. 145-174. Oxford University Press, Oxford (1988).
5. Brederode FT, Linthorst HJM, Bol JF: Differential induction of acquired resistance and PR gene expression in tobacco by virus infection, ethephon treatment, UV light and wounding. Plant Mol Biol 17: 1117-1125 (1991).
6. Broekaert W, Lee H-I, Kush A, Chua N-H, Raikhel N: Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis). Proc Natl Acad Sci USA 87: 7633-7637 (1990).
7. Broglie K, Biddle P, Cressman R, Broglie R: Functional analysis of DNA sequences responsible for ethylene regulation of a bean chitinase gene in transgenic tobacco. Plant Cell 1: 599-607 (1989).
8. Büchter R, Strömberg A, Schmelzer E, Kombrink E: Primary structure and expression of acidic (class II) chitinase in potato. Plant Mol Biol 35: 749-761 (1997).
9. Chen EY, Seeburg PH: Supercoil sequencing: a fast and simple method for sequencing plasmid DNA. DNA 4: 165-170 (1985).
10. Collinge DB, Kragh KM, Mikkelsen JD, Nielsen KK, Rasmussen U, Vad K: Plant chitinases. Plant J 3: 31-40 (1993).
11. Dellaporta SL, Wood J, Hicks JB: A plant DNA minipreparation: version II. Plant Mol Biol Rep 1: 19-21 (1983).
12. Devereux J, Haeberli P, Smithies O: A comprehensive set of sequence analysis programs for the VAX. Nucl Acids Res 12: 387-395 (1984).
13. Eyal Y, Fluhr R: Cellular and molecular biology of pathogenesis-related proteins. Oxford Surv Plant Mol Cell Biol 7: 223-254 (1991).
14. Frohmann MA, Dush MK, Martin GR: Rapid amplification of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci USA 85: 8998-9002 (1988).
15. Garcia-Garcia F, Schmelzer E, Hahlbrock K, Roxby R: Differential expression of chitinase and β-1,3-glucanase genes in various tissues of potato plants. Z Naturforsch 49c: 195-203 (1994).
16. Graham LS, Sticklen MB: Plant chitinases. Can J Bot 72: 1057-1083 (1994).
17. Jach G, Görnhardt B, Mundy J, Logemann J, Pinsdorf E, Leah R, Schell J, Maas C: Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco. Plant J 8: 97-109 (1995).
18. Joshi CP: Putative polyadenylation signals in nuclear genes of higher plants: a compilation and analysis. Nucl Acids Res 15: 9627-9640 (1987).
19. Keefe D, Hinz U, Meins F Jr: The effect of ethylene on the cell-type-specific and intracellular localization of β-1,3-glucanase and chitinase in tobacco leaves. Planta 182: 43-51 (1990).
20. Kombrink E, Beerhues L, Garcia-Garcia F, Hahlbrock K, Müller M, Schröder M, Witte B, Schmelzer E: Expression patterns of defense-related genes in infected and uninfected plants. In: Fritig B, Legrand M (eds) Mechanisms of Plant Defense Responses, vol 2, pp. 236-249. Kluwer Academic Publishers, Dordrecht, Netherlands (1993).
21. Kombrink E, Schröder M, Hahlbrock K: Several 'pathogenesis-related' proteins in potato are 1,3-β-glucanases and chitinases. Proc Natl Acad Sci USA 85: 782-786 (1988).
22. Kombrink E, Somssich IE: Defense responses of plants to pathogens. In: Andrews JH, Tommerup IC (eds) Advances in Botanical Research (incorporating Advances in Plant Pathology), vol 21, pp. 1-34. Academic Press, London (1995).
23. Kombrink E, Somssich IE: Pathogenesis-related proteins and plant defense. In: Carroll G, Tudzynski P (eds) The Mycota, Vol 5 Part A, Plant Relationships, pp. 107-128. Springer-Verlag, Berlin/Heidelberg (1997).
24. Lamb CJ, Ryals JA, Ward ER, Dixon RA: Emerging strategies for enhancing crop resistance to microbial pathogens. Bio/technology 10: 1436-1445 (1992).
25. Laurière M, Laurière C, Chrispeels MJ, Johnson KD, Sturm A: Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins. Plant Physiol 90: 1182-1188 (1989).
26. Leah R, Tommerup H, Svendsen I, Mundy J: Biochemical and molecular characterization of three barley seed proteins with antifungal properties. J Biol Chem 266: 1564-1573 (1991).
27. Linthorst HJM, van Loon LC, van Rossum CMA, Mayer A, Bol JF, van Roekel JSC, Meulenhoff EJS, Cornelissen BJC: Analysis of acidic and basic chitinases from tobacco and petunia an their constitutive expression in transgenic tobacco. Mol Plant-Microbe Interact 3: 252-258 (1990).
28. Lotan T, Ori N, Fluhr R: Pathogenesis-related proteins are developmentally regulated in tobacco flowers. Plant Cell 1: 881-887 (1989).
29. Mauch F, Mauch-Mani B, Boller T: Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and 1,3-β-glucanase. Plant Physiol 88: 936-942 (1988).
30. Mauch F, Meehl JB, Staehelin LA: Ethylene-induced chitinase and β-1,3-glucanase accumulate specifically in the lower epidermis and along vascular strands of bean leaves. Planta 186: 367-375 (1992).
31. Meins F Jr, Neuhaus J-M, Sperisen C, Ryals J: The primary structure of plant pathogenesis-related glucanohydrolases and their genes. In: Boller T, Meins F Jr (eds) Genes Involved in Plant Defense, pp. 245-282. Springer-Verlag, Vienna (1992).
32. Melchers LS, Apotheker-de Groot M, van der Knaap JA, Ponstein AS, Sela-Buurlage MB, Bol JF, Cornelissen BJC, van den Elzen PJM, Linthorst HJM: A new class of tobacco chitinase homologous to bacterial exo-chitinases displays antifungal activity. Plant J 5: 469-480 (1994).
33. Memelink J, Linthorst HJM, Schilperoort RA, Hoge JHC: Tobacco genes encoding acidic and basic isoforms of pathogenesis-related proteins display different expression patterns. Plant Mol Biol 14: 119-126 (1990).
34. Neuhaus J-M, Sticher L, Meins F Jr, Boller T: A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole. Proc Natl Acad Sci USA 88: 10362-10366 (1991).
35. Ori N, Sessa G, Lotan T, Himmelhoch S, Fluhr R: A major stylar matrix polypeptide (sp41) is a member of the pathogenesis-related proteins superclass. EMBO J 9: 3429-3436 (1990).
36. Samac DA, Hironaka CM, Yallaly PE, Shah DM: Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thaliana. Plant Physiol 93: 907-914 (1990).
37. Samac DA, Shah DM: Developmental and pathogen-induced activation of the Arabidopsis acidic chitinase promoter. Plant Cell 3: 1063-1072 (1991).
38. Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Plainview, NY (1989).
39. Schröder M, Hahlbrock K, Kombrink E: Temporal and spatial patterns of 1,3-β-glucanase and chitinase induction in potato leaves infected by Phytophthora infestans. Plant J 2: 161-172 (1992).
40. Sela-Buurlage MB, Ponstein AS, Bres-Vloemans SA, Melchers LS, van den Elzen PJM, Cornelissen BJC: Only specific tobacco (Nicotiana tabacum) chitinases and β-1,3-glucanases exhibit antifungal activity. Plant Physiol 101: 857-863 (1993).
41. Shinshi H, Mohnen D, Meins F Jr: Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc Natl Acad Sci USA 84: 89-93 (1987).
42. Somssich IE: Regulatory elements governing pathogenesis-related (PR) gene expression. In: Nover L (ed), Results and Problems in Cell Differentiation, vol 20, pp. 163-179. Springer-Verlag, Berlin/Heidelberg (1994).
43. Sticher L, Hofsteenge J, Neuhaus J-M, Boller T, Meins F Jr: Posttranslational processing of a new class of hydroxyproline-containing proteins. Prolyl hydroxylation and C-terminal cleavage of tobacco (Nicotiana tabacum) vacuolar chitinase. Plant Physiol 101: 1239-1247 (1993).
44. van Hengel AJ, Guzzo F, van Kammen A, de Vries SC: Expression pattern of the carrot EP3 endochitinase genes in suspension cultures and in developing seeds. Plant Physiol 117: 43-53 (1998).
45. van Holst G-J, Varner JE: Reinforced polyprolin II conformation in a hydroxyproline-rich cell wall glycoprotein from carrot root. Plant Physiol 74: 247-251 (1984).
46. von Heijne G: Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 133: 17-21 (1983).
47. Ward ER, Uknes SJ, Williams SC, Dincher SS, Wiederhold DL, Alexander DC, Ahl-Goy P, Metraux J-P, Ryals JA: Coordinate gene activity in response to agents that induce systemic acquired resistance. Plant Cell 3: 1085-1094 (1991).
48. Wemmer T, Kaufmann H, Kirch H-H, Schneider K, Lottspeich F, Thompson RD: The most abundant soluble basic protein of the stylar transmitting tract in potato (Solanum tuberosum L.) is an endochitinase. Planta 194: 264-273 (1994).
49. Wessels JGH, Sietsma JH: Fungal cell walls: a survey. In: Tanner W, Loewus FA (eds) Encyclopedia of Plant Physiology, New Series, vol 13B, Plant Carbohydrates II, pp. 352-394. Springer-Verlag, Berlin (1981).
50. Witte B, Hahlbrock K, Kombrink E: Purification, characterization of tree types of chitinase from potato leaves that differ in expression and cellular localization. In preparation.
51. Zhu Q, Doerner PW, Lamb CJ: Stress induction and developmental regulation of a rice chitinase promoter in transgenic tobacco. Plant J 3: 203-212 (1993).
52. Zhu Y, Maher EA, Masoud S, Dixon RA, Lamb CJ: Enhanced protection against fungal attack by constitutive coexpression of chitinase and glucanase genes in transgenic tobacco. Bio/technology 12: 807-812 (1994).