Plant Protect. Sci., 2002, 38(11):469-473 | DOI: 10.17221/10526-PPS
Chitinases and endoglucanases synthesized in the infected barley leaves in the powdery mildew period sporulation
- 1 Department of Genetics and
- 2 Department of Plant Physiology, Faculty of Natural Sciences, Comenius University, 842 15 Bratislava, Slovakia E-mail: hlinkova@fns.uniba.sk
In our work, we represent genetic, molecular and biochemical changes induced in the infected barley leaves induced in the period pathogen sporulation. We studied a presence of acidic β-1,3-endoglucanases and chitinases in an intracellular fluid isolated from primary barley leaves infected with two powdery mildew pathotypes carrying various virulence genes. In the period of pathogen sporulation acidic β-1,3-endoglucanases (Glu) and chitinases (Chi) isozymes were synthesized in two main groups. Non-specific, high molecular group of these enzymes with Mr > 200 kDa did not differ genetic differences between host and pathogen. Specific, low molecular forms reflected both genetic background of host and pathogen as well as biochemical status of the disease. Low molecular acidic Glu had Mr from interval 9-12 kDa. Analogical situation was observed for low molecular chitinases. Their molecular masses were from interval 14.4-15.5 kDa. Intracellular fluid from the primary leaves of the healthy plants did not contained detectable amount of these enzymes. Appearance of low molecular forms of Glu and Chi is discussed.
Keywords: barley; acid proteins; chitinases; acid endoglucanases; powdery mildew
Published: December 31, 2002 Show citation
ACS | AIP | APA | ASA | Harvard | Chicago | Chicago Notes | IEEE | ISO690 | MLA | NLM | Turabian | Vancouver |
References
- B IELY P., M ARKOVIČ O., M ISLOVIČOVÁ D. (1985): Sensitive detection of endo-1,4-β-glucanases and endo-1,4-β-xylanases in gels. Anal. Biochem., 144: 147-151.
Go to original source...
Go to PubMed...
- BRADFORD M.M. (1976): A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-day binding. Anal. Biochem., 72: 248-254.
Go to original source...
- CORNELISSEN B.J.C., MELCHERS L.S. (1993): Strategies for control of fungal diseases with transgenic plants. Plant Physiol., 101: 709-712.
Go to original source...
Go to PubMed...
- CÔTÉ F., LETARTE J., GRENIER J., TRUDEL J., ASSELIN A. (1989): Detection of β-1,3-glucanase activity after native polyacrylamide gel electrophoresis: Application to tobacco pathogenesis-related proteins. Electrophoresis, 10: 527-529.
Go to original source...
Go to PubMed...
- HAM K.S., WU S.CH., DARVIL A.G., ALBERSHEIM P. (1997): Fungal pathogens secrete an inhibitor protein that distinguishes isoforms of plant pathogenesis-related endo-β-1,3-glucanases. Plant J., 11: 169-179.
Go to original source...
- HARTLEB H., HEITEFUSS R., HOPPE H.-H. (1997): Resistance of crop plants against fungi. Gustav Fischer Verlag, Jena, Stuttgart, Lübeck, Ulm.
- HLINKOVÁ E., ONDŘEJ M. (1994): Changes in protein spectra of transgenic plants carrying different Agrobacterium tumefaciens C58 T-DNA genes. Biol. Plant., 36: 29-36.
Go to original source...
- HLINKOVÁ E., SÝKORA M., ©UBR Z. (1995): Content of soluble proteins in the barley leaves after powdery mildew (Erysiphe graminis f.sp. hordei Marchal) infection. Agriculture, 41: 597-613.
- LAEMMLI U.K. (1970): Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
Go to original source...
Go to PubMed...
- LEUBNER-METZGER G., MEINS F. Jr. (2000): Sense transformation reveals a novel role for class I β-1,3-glucanases (PR-2). In: DATTA S.K., MUTHUKRISHNAN S. (eds): Pathogenesis-related Proteins in Plants. CRC Press, Boca Raton, Forida: 49-76.
- LEUBNER-METZGER G., FRÜNDT C., VÖGELI-LANGE R., MEINS F. JR. (1995): Class I β-1,3-glucanases in endosperm of tobacco during germination. Plant Physiol., 109: 751-759.
Go to original source...
Go to PubMed...
- MELCHERS L.S., STUIVER M.H. (2000): Novel genes for disease-resistance breeding. Curr. Opin. Plant Biol., 3: 147-152.
Go to original source...
Go to PubMed...
- MEMELINK J., LINGHORST H.J.M., SCHILPEROORT R.A., HOGE J.H.C. (1990): Tobacco genes encoding acidic and basic isoforms of pathogenesis-related proteins display different expresion patterns. Plant Mol. Biol., 14: 119-126.
Go to original source...
Go to PubMed...
- N ESTERENKO M.V., T ILLEY M., U PTON S.J. (1994): A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels. J.B.B. Methods, 28: 239-242.
Go to original source...
Go to PubMed...
- PAN Q.S., YE S., KUÇ J. (1991): A technique for detection of chitinase, β-1,3-glucanases and protein patterns after a single separation using polyacrylamide gel electrophoresis and isoelectrofocusin. Phytopathology, 81: 970-974.
Go to original source...
- PAYNE G., RYALS J. (1990): Evidence for a third structural class of β-1,3-glucanase in tobacco. Plant Mol. Biol., 15: 797-808.
Go to original source...
Go to PubMed...
- REPKA V. (1997): Intra and extracellular isoforms of PR-3 class chitinase in virus-infected cucumber plants. Acta Vir., 41: 71-75.
- R EPKA V., K OLLEROVÁ E., S LOVÁK M. (1993): The extracellular acidic and basic virus-elicited proteins in cucumber cotyledons. Biol. Plant., 35: 87-93.
Go to original source...
- REZZONICO E., FLURY N., MEINS F. JR., BEFFA R. (1998): Transcriptional down-regulation by abscisic acid of pathogenesis-related β-1,3-glucanase genes in tobacco cell culture. Plant Physiol., 117: 585-592.
Go to original source...
Go to PubMed...
- SELA-BUURLAGE M.B., PONSTEIN A.S., BRES-VLOEMANS S.A., MELCHERS L.S., VAN DEN ELZEN P.J.M., CORNELISSEN B.J.C. (1993): Only specific tobacco (Nicotiana tabacum) chitinases and β-1,3-glucanases exhibit antifungal activity. Plant Physiol., 101: 857-863.
Go to original source...
Go to PubMed...
- S CHWARZBACH E., F ISCHBECK G. (1981): Die Mehltauresistenz von Sommer und Winter Sorten in BRR. Z.P.-Zucht., 87: 309-318.
- SHINSHI H., NEUHAUS J.M., RYALS J., MEINS F. JR. (1990): Structure of a tobacco endochitinase gene: Evidence that different chitinase genes can arrise by transposition of sequences encoding a cystein-rich domain. Plant Mol. Biol., 14: 357-368.
Go to original source...
Go to PubMed...
- TAIRA T., OHNUMA T., YAMAGAMI T., ASO Y., ISHIGURO H., ISHIHARA M. (2002): Antifungal activity of rye (Secale cereale) seed chitinases: The different binding manner of class I and class II chitinases to the fungal cell walls. Biosci. Biotech. Biochem., 66: 970-977.
Go to original source...
Go to PubMed...
- TRUDEL J., ASSELIN A. (1989): Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal. Bioch., 178: 362-366.
Go to original source...
Go to PubMed...
- VAN LOON L.C. (1985): Pathogenesis-related proteins. Plant Mol. Biol., 4: 111-116.
Go to original source...
Go to PubMed...
- VAN LOON L.C., VAN STRIEN E.A. (1999): The families of pathogenesis-related proteins, their activities and comparative analysis of PR-1 type proteins. Physiol. Mol. Plant Pathol., 55: 85-97.
Go to original source...
- VÖGELI-LANGE R., FRUNDT C., HART C.M., NAGY F., MEINS F. JR. (1994): Developmental, hormonal and pathogenesis-regulated regulation of the tobacco class I β-1,3-glucanase B promotor. Plant Mol. Biol., 25: 299-311.
Go to original source...
Go to PubMed...
- W U CH.T., L EUBNER -M ETZGER G., M EINS F. J R., BRADFORD K.J. (2001): Class I beta-1,3-glucanase and chitinase are expressed in the micropylar endosperm of tomato seeds prior to radicle emergence. Plant Physiol., 126: 1299-1313.
Go to original source...
Go to PubMed...
This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International (CC BY NC 4.0), which permits non-comercial use, distribution, and reproduction in any medium, provided the original publication is properly cited. No use, distribution or reproduction is permitted which does not comply with these terms.