Characterization and in vitro expression patterns of extracellular degradative enzymes from non-pathogenic binucleate Rhizoctonia AG-G

Many filamentous fungi produce an array of extracellular enzymes that acting in cell walls release elicitors of the plant defense response These enzymes may therefore be important in biocontrol applications. The aim of this study was to characterize extracellular degradative enzymes produced by a no...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autor principal: MacHinandiarena, M.F
Otros Autores: Wolski, E.A, Barrera, V., Daleo, G.R, Andreu, A.B
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2005
Acceso en línea:Registro en Scopus
DOI
Handle
Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
LEADER 15014caa a22014897a 4500
001 PAPER-4159
003 AR-BaUEN
005 20230518203340.0
008 140217s2005 xx ||||fo|||| 00| 0 eng|d
024 7 |2 scopus  |a 2-s2.0-19944369442 
024 7 |2 pubmed  |a 15883731 
024 7 |2 cas  |a carboxylesterase, 59536-71-9, 83380-83-0, 9016-18-6, 9028-01-7; glucan 1,3 beta glucosidase, 9073-47-6; glucose, 50-99-7, 84778-64-3; glycosidase, 9032-92-2; laminaran, 9008-22-4; pectin, 9000-69-5; pectinesterase, 9025-98-3; polygalacturonase, 9023-92-1, 9032-75-1; pustulan, 37331-28-5; Carboxylic Ester Hydrolases, EC 3.1.1.-; Culture Media; Glucan 1,3-beta-Glucosidase, EC 3.2.1.58; Glucose, 50-99-7; Glycoside Hydrolases, EC 3.2.1.-; laminaran, 9008-22-4; pectin, 9000-69-5; pectinesterase, EC 3.1.1.11; Pectins; Polygalacturonase, EC 3.2.1.15; Polysaccharides; pustulan, 37331-28-5 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a MYCPA 
100 1 |a MacHinandiarena, M.F. 
245 1 0 |a Characterization and in vitro expression patterns of extracellular degradative enzymes from non-pathogenic binucleate Rhizoctonia AG-G 
260 |c 2005 
270 1 0 |m Andreu, A.B.; Facultad de Ciencias Exactas Y Naturales, Instituto de Investigaciones Biològicas, Universidad Nacional de Mar del Plata, Casilla de correo 1245, 7600 Mar del Plata, Buenos Aires, Argentina; email: abandreu@mdp.edu.ar 
506 |2 openaire  |e Política editorial 
504 |a Burpee, L.L., Goulty, L.G., Suppression of brown patch disease of creeping bentgrass by isolates of nonpathogenic Rhizoctonia spp (1984) Phytopathology, 74, pp. 692-694 
504 |a Cardoso, J.E., Echandi, E., Nature of Protection of bean seedlings from Rhizoctonia root rot by a binucleate Rhizoctonia-like fungus (1987) Phytopathology, 77, pp. 1548-1551 
504 |a Harris, A.R., Schisler, A., Neate, S.M., Ryder, M.H., (1994) Suppression of Damping-of Caused by Rhizoctonia Solani, and Growth Promotion, in Bedding Plants by Binucleate Rhizoctonia spp., 26 (2), pp. 263-268 
504 |a Ichielevich-Auster, M., Snech, B., Koltin, Y., Barash, I., Suppression of damping off caused by Rhizoctonia spp, by non-pathogenic R. solani (1985) Phytopathology, 75, pp. 1080-1084 
504 |a Herr, L.J., Biological control of Rhizoctonia solani by binucleate Rhizoctonia spp and hypovirulent R. solani (1995) Crop Protect, 14, pp. 179-187 
504 |a Escande, A., Echandi, E., Protection of potato from Rhizoctonia cancker with binucleate Rhizoctonia fungi (1991) Plant Pathol, 40, pp. 197-202 
504 |a Sneh, B., Ichielevich-Auster, M., Shomer, S., Comparative anatomy of colonization of cotton hypocotyls and roots by virulent and hypovirulent isolates of Rhizoctonia solani (1989) Can J Bot, 67, pp. 2142-2149 
504 |a Sneh, B., Ichielevich-Auster, M., Plaut, Z., Mechanisms of seedling protection induced by a hypovirulent isolate of Rhizoctonia solani (1989) Can J Bot, 67, pp. 2135-2141 
504 |a Xue, L., Charest, P.M., Jabaji-Hare, S.H., Systemic induction of peroxidases, 1,3-β-glucanases, chitinases, and resistance in bean plants by binucleate Rhizoctonia species (1998) Phytopathology, 88, pp. 359-365 
504 |a Sneh, B., Ichielevich-Auster, M., Induced resistance of cucumber seedlings caused by some non-pathogenic Rhizoctonia (np-R) isolates (1998) Phytoparasitica, 26, pp. 27-38 
504 |a Hwang, J., Benson, D.M., Expression of induced systemic resistanse in poinsettia cuttings against Rhizoctonia stem by treatment of stock plants with binucleate Rhizoctonia (2003) Biol Control, 27, pp. 73-80 
504 |a Poromarto, S.H., Nelson, B.D., Freeman, T.P., Association of binucleate Rhizoctonia with soybean and mechanism of biocontrol of Rhizoctonia solani (1998) Phytopathology, 88, pp. 1056-1067 
504 |a Buzi, A., Chilosi, G., Timperio, A.M., Zolla, L., Rosssall, S., Magro, P., Polygalacturonase produced by Botrytis fabae as elicitor of two furanoacetylenic phytoalexins in Vicia faba pods (2003) J Plant Pathol, 85, pp. 11-116 
504 |a Isshiki, A., Akimitsu, K., Ishii, H., Yamamoto, H., Purification of polygalacturonases produced by the pear scab pathogens, Venturia nashicola and Venturia pirina (2000) Physiol. Mol. Plant Pathol, 56, pp. 263-271 
504 |a Di Pietro, A., Roncero, M.I.G., Endopolygalacturonase from Fusarium oxysporum f.sp. lycpersici: Purification, characterization, and production during infection of tomato plants (1996) Phytopathology, 86, pp. 1324-1330 
504 |a Hung, Q., Allen, C., An exo-poly-α-D-galacturonidase, PehB, is required for wild-type virulence in Ralstonia solanacearum (2000) Physiol Mol Plant Pathol, 57, pp. 77-83 
504 |a Oeser, B., Heidrich, P.M., Muller, U., Tudzynski, P., Tenberge, K.B., Polygalacturonase is a pathogenecity factor in the Claviceps purpurea rye interaction (2002) Fungal Genet Biol, 36, pp. 176-186 
504 |a Ten Have, A., Mulder, W., Visser, J., Van Kan, J.A.L., The endopolygalacturonase gene Bcpg 1 is required for full virulence of Botrytis cinerea (1998) Mol Plant-Microbe Interactions, 11, pp. 1009-1016 
504 |a Collmer, A., Keen, N.T., The role of pectic enzymes in plant pathogenesis (1986) Annu Rev Phytopathol, 24, pp. 383-409 
504 |a Bruce, R.J., West, C.A., Elicitation of casbene-synthetase activity in castor bean. The role of pectic fragments of the plant cell wall in elicitation by a fungal endopolygalacturonase (1982) Plant Physiol, 69, pp. 1181-1188 
504 |a Ovidio R, D., Mattei, B., Roberti, S., Bellicampi, D., Polygalacturonases, polygalacturonase-inhibiting proteins and pectic oligomers in plant-pathogen interactions (2004) Biochimica et Biophysica Acta, 1696, pp. 237-244 
504 |a Bourdat, G., Lafitte, C., Barthe, J.P., Frasez, D., Esquerrè- Tugayè, M.T., Differential elicitation of defense responses by pectic fragments in bean seedlings (1998) Planta, 206, pp. 86-94 
504 |a Annis, S.L., Goodwin, P.H., Recent advances in the molecular genetics of plant cell wall-degrading enzymes produced by plant pathogenic fungi (1997) Eur J Plant Pathol, 103, pp. 1-14 
504 |a Schaeffer, H.J., Leykam, J., Walton, J.D., Cloning and targeted gene disruption of EXG1, encoding exo-β 1,3-glucanase, in the phytopathogenic fungus Cochliobolus carbonum (1994) Appl Enviro Microbiol, 60, pp. 594-598 
504 |a Jabaji-Hare, S., Chamberland, H., Charest, P.M., Cell wall alterations in hypocotyls of bean seedlings protected from Rhizoctonia stem canker by a binucleate Rhizoctonia isolate (1999) Mycol Res, 103, pp. 1035-1043 
504 |a Marcus, L., Barash, I., Snech, B., Koltin, Y., Finkler, A., Purification and characterization of pectolytic enzymes produced by virulent and hypovirulent isolates of Rhizoctonia solani Kühn (1986) Physiol Mol Plant Pathol, 29, pp. 325-336 
504 |a Sneh, B., Ichielevich-Auster, M., Shomer, I., Comparative anatomy of colonization of cotton hypocotyls and roots by virulent and hypovirulent isolates of Rhizoctonia solani (1989) Can J Bot., 67, pp. 2135-2141 
504 |a Maxwell, D.P., Lumsden, R., Oxalic, D., Acid production by Sclerotinia sclerotiorum in infected bean and in culture (1970) Phytopathology, 60, pp. 1395-1398 
504 |a Milner, Y., Avigard, G., A cooper reagent for determination of hexuronic acid and certain ketohexoses (1967) Carbohydr Res, 4, pp. 359-363 
504 |a Nelson, N., A photometric adaptation of the Somogyi method for the determination of glucose (1944) J Biol Chem, 153, pp. 375-380 
504 |a Somogyi, M., Notes on sugar determination (1952) J Biol Chem, 195, pp. 19-23 
504 |a Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A., Smith, F., Colorimetric method for determination of sugars and related substances (1956) Anal Chem, 28, pp. 350-356 
504 |a Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacterioophage T4 (1970) Nature, 227, pp. 680-685 
504 |a Oakley, B.R., Kirsch, D.R., Morris, N.R., A simplified ultrasensitive silver stain for detecting proteins in poliacrylamide gels (1980) Ann Biochem, 105, pp. 361-363 
504 |a Ried, J.L., Collmer, A., Activity stain for rapid characterization of pectic enzymes in isoelectric focusing and sodium dodecyl sulfate-polyacrylamide Gels (1985) Appl Environ Microbiol, 50, pp. 615-622 
504 |a Cruisckshank, R., Wade, G., Detection of pectic enzymes in pectin acrylamide gels (1980) Anal Biochem, 107, pp. 177-181 
504 |a Soler, A., De La Cruz, J., Llobell, A., Detection of β-1, 6-glucanase isozymes from Trichoderma strains in sodium dodecyl sulphate-polyacrylamide gel electrophoresis and isoelectrofocusing gels (1999) J Microbiol Methods, 35, pp. 245-251 
504 |a Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, Ak, Gartner, F.H., Provenzano, M.D., Klenk, D.L., Measurement of protein using bicinchoninic acid (1985) Anal Biochem, 150, pp. 76-85 
504 |a Smith, R.J., Grula, Chitinase is an inducible enzyme Beauveria bassiana (1983) J Invertebr Pathol, 42, pp. 329-326 
504 |a Sandhya, C., Adapa, L.K., Nampoothiri, K.M., Binod, P., Szakacs, G., Pandey, A., Extracellular chitinase production by Trichoderma harzianum in submerged fermentation (2004) Journal of Basic Microbiology, 44, pp. 49-58 
504 |a Yalpani, M., (1988) Polysaccharides: Synthesis, Modification and Structure-Property Relations, , Elsevier, Amsterdan 
504 |a Lindberg, B., McPherson, J., Studies on the chemistry of lichens. VI. The structure of pustulan (1954) Acta Chem Scand, 8, pp. 985-988 
504 |a Lloyd, P.F., Pon, G., Stacey, M., (1956) Chem Ind, pp. 172-173. , (London) 
504 |a Manners, D.J., Masson, A.J., Patterson, J., The structure of a beta-(1 leads to 3)-D-glucan from yeast cell walls (1973) Biochem J, 135, pp. 19-30 
504 |a Reese, E., Parrish, F., Mandels, M., β 1-6 glucanases in fungi (1962) Can J Microbiol, 8, pp. 327-334 
504 |a Pitson, S., Seviour, R., McDougall, B., Stone, B., Sadek, M., Purification and characterization of an extracellular (1→6)-β-glucanase from the filamentous fungus Acremonium persicinum (1996) Biochem J, 316, pp. 841-846 
504 |a Cabib, E., Bowers, B., Sburlati, A., Silverman, S.J., Fungal cell wall synthesis: The construction of a biological structure (1988) Microbiol Sci, 5, pp. 370-375 
504 |a Wessels, J.G., Wall growth, protein excretion and morphogenesis in fungi (1993) New Phytol, 123, pp. 397-413 
504 |a Papavizas, C., Trichoderma and Glicocadium: Biology, ecology and potential for biocontrol (1985) Annu Rev Phytopatol, 23, pp. 23-54 
504 |a Elad, Y., Chet, I., Henis, Y., Degradation of plant pathogenic fungi by Trichoderma harzianum (1982) Can J Microbiol, 28, pp. 719-725 
504 |a Villajuan-Abgona, R., Kageyama, R., Hyakumachi, M., Biocontrol of Rhizoctonia damping off of cucumber by non-pathogenic binucleata Rhizoctonia (1996) Eur J Plant Pathol, 102, pp. 227-235 
520 3 |a Many filamentous fungi produce an array of extracellular enzymes that acting in cell walls release elicitors of the plant defense response These enzymes may therefore be important in biocontrol applications. The aim of this study was to characterize extracellular degradative enzymes produced by a non-pathogenic binucleate isolate of Rhizoctonia AG-G. The fungus was grown in liquid culture supplemented with pectin, polygalacturonic acid or glucose as a carbon sources and filtrates of the culture media were analyzed for the detection of pectinolytic and glucan hydrolytic enzymes. Using only pectin as a carbon source, secretion of polygalacturonases and methylesterases was found. When the liquid medium was supplemented with polygalacturonic acid, only polygalacturonase activity was detected. However, when glucose was used as carbon source β-1,3 and β-1,6 glucanases activities were detected, using laminarin and pustulan as substrates, but none of the pectinolytic activities were found. These enzymes were partially purified and characterized. The β-(1,3)(1,6) glucanase and polygalacturonase enzymes showed to be active against cell wall polysaccharides from potato sprouts. These enzymes may have an important role in fungus-plant cell wall interaction. This is the first study about the production of extracellular enzymes by non-pathogenic binucleate Rhizoctonia AG-G. © Springer 2005.  |l eng 
593 |a Facultad de Ciencias Exactas Y Naturales, Instituto de Investigaciones Biològicas, Universidad Nacional de Mar del Plata, Casilla de correo 1245, 7600 Mar del Plata, Buenos Aires, Argentina 
593 |a Instituto de Microbiologìa Y Zoologìa Agrìcola, CNIA-INTA, Castelar, Casilla de correo 25, 1712 Castelar, Buenos Aires, Argentina 
690 1 0 |a CELL WALL POLYSACCHARIDES 
690 1 0 |a GLUCANASES 
690 1 0 |a PECTIN METHYL ESTERASES 
690 1 0 |a POLYGALACTURONASES 
690 1 0 |a POTATO SPROUTS 
690 1 0 |a CARBOXYLESTERASE 
690 1 0 |a GLUCAN 1,3 BETA GLUCOSIDASE 
690 1 0 |a GLUCOSE 
690 1 0 |a GLYCOSIDASE 
690 1 0 |a LAMINARAN 
690 1 0 |a PECTIN 
690 1 0 |a PECTINESTERASE 
690 1 0 |a POLYGALACTURONASE 
690 1 0 |a POLYSACCHARIDE 
690 1 0 |a PUSTULAN 
690 1 0 |a ARTICLE 
690 1 0 |a CELL WALL 
690 1 0 |a CULTURE MEDIUM 
690 1 0 |a ENZYME SPECIFICITY 
690 1 0 |a ENZYMOLOGY 
690 1 0 |a GROWTH, DEVELOPMENT AND AGING 
690 1 0 |a HYPHOMYCETES 
690 1 0 |a METABOLISM 
690 1 0 |a MICROBIOLOGY 
690 1 0 |a POTATO 
690 1 0 |a CARBOXYLIC ESTER HYDROLASES 
690 1 0 |a CELL WALL 
690 1 0 |a CULTURE MEDIA 
690 1 0 |a GLUCAN 1,3-BETA-GLUCOSIDASE 
690 1 0 |a GLUCOSE 
690 1 0 |a GLYCOSIDE HYDROLASES 
690 1 0 |a PECTINS 
690 1 0 |a POLYGALACTURONASE 
690 1 0 |a POLYSACCHARIDES 
690 1 0 |a RHIZOCTONIA 
690 1 0 |a SOLANUM TUBEROSUM 
690 1 0 |a SUBSTRATE SPECIFICITY 
690 1 0 |a FUNGI 
690 1 0 |a HYPHOMYCETES 
690 1 0 |a RHIZOCTONIA 
690 1 0 |a SOLANUM TUBEROSUM 
700 1 |a Wolski, E.A. 
700 1 |a Barrera, V. 
700 1 |a Daleo, G.R. 
700 1 |a Andreu, A.B. 
773 0 |d 2005  |g v. 159  |h pp. 441-448  |k n. 3  |p Mycopathologia  |x 0301486X  |t Mycopathologia 
856 4 1 |u http://www.scopus.com/inward/record.url?eid=2-s2.0-19944369442&partnerID=40&md5=f70ad364bb1fdf2116395c5e8a63b6de  |y Registro en Scopus 
856 4 0 |u https://doi.org/10.1007/s11046-005-0253-5  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_0301486X_v159_n3_p441_MacHinandiarena  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0301486X_v159_n3_p441_MacHinandiarena  |y Registro en la Biblioteca Digital 
961 |a paper_0301486X_v159_n3_p441_MacHinandiarena  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
963 |a VARI 
999 |c 65112