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F. Martin - One of the best experts on this subject based on the ideXlab platform.
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Immunolocalization of hydrophobin HYDPt‐1 from the ectomycorrhizal basidiomycete Pisolithus tinctorius during colonization of Eucalyptus globulus roots
New Phytologist, 2020Co-Authors: Denis Tagu, R De Bellis, Raffaella Balestrini, Paola Bonfante, O M H De Vries, Giovanni Piccoli, Vilberto Stocchi, F. MartinAbstract:• The immunolocalization of one of the hydrophobins of Pisolithustinctorius (HYDPt-1) is reported. Hydrophobin proteins play key roles in adhesion and aggregation of fungal hyphae, and it is already known that formation of ectomycorrhizas on eucalypt roots enhances the accumulation of hydrophobin mRNAs in the mycelium of Pisolithus tinctorius. • Purification of SDS-insoluble proteins from the mycelium of P. tinctorius showed the presence of a 13 kDa polypeptide with properties of class I hydrophobin. • Polyconal antibodies were raised against a recombinant HYDPt-1 polypeptide, and these were used for immunofluorescence-coupled transmission electron microscopy. • HYDPt-1 is a cell wall protein located at the surface of the hyphae with no preferential accumulation in the fungal cells of the different tissues of the ectomycorrhiza (i.e. extraradical hyphae, mantle or Hartig net).
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immunolocalization of hydrophobin hydpt 1 from the ectomycorrhizal basidiomycete Pisolithus tinctorius during colonization of eucalyptus globulus roots
New Phytologist, 2001Co-Authors: Denis Tagu, R De Bellis, Raffaella Balestrini, Paola Bonfante, O M H De Vries, Giovanni Piccoli, Vilberto Stocchi, F. MartinAbstract:• The immunolocalization of one of the hydrophobins of Pisolithustinctorius (HYDPt-1) is reported. Hydrophobin proteins play key roles in adhesion and aggregation of fungal hyphae, and it is already known that formation of ectomycorrhizas on eucalypt roots enhances the accumulation of hydrophobin mRNAs in the mycelium of Pisolithus tinctorius. • Purification of SDS-insoluble proteins from the mycelium of P. tinctorius showed the presence of a 13 kDa polypeptide with properties of class I hydrophobin. • Polyconal antibodies were raised against a recombinant HYDPt-1 polypeptide, and these were used for immunofluorescence-coupled transmission electron microscopy. • HYDPt-1 is a cell wall protein located at the surface of the hyphae with no preferential accumulation in the fungal cells of the different tissues of the ectomycorrhiza (i.e. extraradical hyphae, mantle or Hartig net).
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a novel class of ectomycorrhiza regulated cell wall polypeptides in Pisolithus tinctorius
Molecular Plant-microbe Interactions, 1999Co-Authors: P Laurent, Denis Tagu, Catherine Voiblet, D De Carvalho, Uwe Nehls, R De Bellis, Raffaella Balestrini, G Bauw, Paola Bonfante, F. MartinAbstract:Development of the ectomycorrhizal symbiosis leads to the aggregation of fungal hyphae to form the mantle. To identify cell surface proteins involved in this developmental step, changes in the biosynthesis of fungal cell wall proteins were examined in Eucalyptus globulus-Pisolithus tinctorius ectomycorrhizas by two-dimensional polyacrylamide gel electrophoresis. Enhanced synthesis of several immunologically related fungal 31- and 32-kDa polypeptides, so-called symbiosis-regulated acidic polypeptides (SRAPs), was observed. Peptide sequences of SRAP32d were obtained after trypsin digestion. These peptides were found in the predicted sequence of six closely related fungal cDNAs coding for ectomycorrhiza up-regulated transcripts. The PtSRAP32 cDNAs represented about 10% of the differentially expressed cDNAs in ectomycorrhiza and are predicted to encode alanine-rich proteins of 28.2 kDa. There are no sequence homologies between SRAPs and previously identified proteins, but they contain the Arg-Gly-Asp (RGD) mo...
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expressed sequence tags of randomly selected cdna clones from eucalyptus globulus Pisolithus tinctorius ectomycorrhiza
Molecular Plant-microbe Interactions, 1995Co-Authors: D Tagu, F. MartinAbstract:: Random sequencing of cDNA clones from Eucalyptus globulus-Pisolithus tinctorius ectomycorrhizal tissues was carried out to generate expressed sequence tags (ESTs). Database comparisons revealed that 42% of the cDNAs corresponded to previously sequenced genes. These ESTs represent efficient molecular markers to analyze changes in gene expression during the formation of the ectomycorrhizal symbiosis.
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Polyphosphatase acitivities in the soluble fraction of mycelial homogenates of Pisolithus tinctorius
Agriculture Ecosystems & Environment, 1990Co-Authors: P. Tillard, N. Bousquet, F. Martin, Daniel Mousain, L. SalsacAbstract:Abstract Activities of acid phosphatase activities in the soluble fraction of Pisolithus tinctorius homogenates, cultured on media with or without Pi 100 μM were assayed using sodium polyphosphates. Phosphatase activities increased with decreasing lengths of polyphosphate chains. Other observations suggested that accumulations of inorganic polyphosphates in P. tinctorius mycelia grown on Pi-rich media may be hydrolyzed by intracellular phosphatases when the phosphorus supply became limiting, a conclusion corroborated by phosphorus-31 nuclear magnetic resonance spectroscopy.
Denis Tagu - One of the best experts on this subject based on the ideXlab platform.
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Immunolocalization of hydrophobin HYDPt‐1 from the ectomycorrhizal basidiomycete Pisolithus tinctorius during colonization of Eucalyptus globulus roots
New Phytologist, 2020Co-Authors: Denis Tagu, R De Bellis, Raffaella Balestrini, Paola Bonfante, O M H De Vries, Giovanni Piccoli, Vilberto Stocchi, F. MartinAbstract:• The immunolocalization of one of the hydrophobins of Pisolithustinctorius (HYDPt-1) is reported. Hydrophobin proteins play key roles in adhesion and aggregation of fungal hyphae, and it is already known that formation of ectomycorrhizas on eucalypt roots enhances the accumulation of hydrophobin mRNAs in the mycelium of Pisolithus tinctorius. • Purification of SDS-insoluble proteins from the mycelium of P. tinctorius showed the presence of a 13 kDa polypeptide with properties of class I hydrophobin. • Polyconal antibodies were raised against a recombinant HYDPt-1 polypeptide, and these were used for immunofluorescence-coupled transmission electron microscopy. • HYDPt-1 is a cell wall protein located at the surface of the hyphae with no preferential accumulation in the fungal cells of the different tissues of the ectomycorrhiza (i.e. extraradical hyphae, mantle or Hartig net).
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immunolocalization of hydrophobin hydpt 1 from the ectomycorrhizal basidiomycete Pisolithus tinctorius during colonization of eucalyptus globulus roots
New Phytologist, 2001Co-Authors: Denis Tagu, R De Bellis, Raffaella Balestrini, Paola Bonfante, O M H De Vries, Giovanni Piccoli, Vilberto Stocchi, F. MartinAbstract:• The immunolocalization of one of the hydrophobins of Pisolithustinctorius (HYDPt-1) is reported. Hydrophobin proteins play key roles in adhesion and aggregation of fungal hyphae, and it is already known that formation of ectomycorrhizas on eucalypt roots enhances the accumulation of hydrophobin mRNAs in the mycelium of Pisolithus tinctorius. • Purification of SDS-insoluble proteins from the mycelium of P. tinctorius showed the presence of a 13 kDa polypeptide with properties of class I hydrophobin. • Polyconal antibodies were raised against a recombinant HYDPt-1 polypeptide, and these were used for immunofluorescence-coupled transmission electron microscopy. • HYDPt-1 is a cell wall protein located at the surface of the hyphae with no preferential accumulation in the fungal cells of the different tissues of the ectomycorrhiza (i.e. extraradical hyphae, mantle or Hartig net).
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a novel class of ectomycorrhiza regulated cell wall polypeptides in Pisolithus tinctorius
Molecular Plant-microbe Interactions, 1999Co-Authors: P Laurent, Denis Tagu, Catherine Voiblet, D De Carvalho, Uwe Nehls, R De Bellis, Raffaella Balestrini, G Bauw, Paola Bonfante, F. MartinAbstract:Development of the ectomycorrhizal symbiosis leads to the aggregation of fungal hyphae to form the mantle. To identify cell surface proteins involved in this developmental step, changes in the biosynthesis of fungal cell wall proteins were examined in Eucalyptus globulus-Pisolithus tinctorius ectomycorrhizas by two-dimensional polyacrylamide gel electrophoresis. Enhanced synthesis of several immunologically related fungal 31- and 32-kDa polypeptides, so-called symbiosis-regulated acidic polypeptides (SRAPs), was observed. Peptide sequences of SRAP32d were obtained after trypsin digestion. These peptides were found in the predicted sequence of six closely related fungal cDNAs coding for ectomycorrhiza up-regulated transcripts. The PtSRAP32 cDNAs represented about 10% of the differentially expressed cDNAs in ectomycorrhiza and are predicted to encode alanine-rich proteins of 28.2 kDa. There are no sequence homologies between SRAPs and previously identified proteins, but they contain the Arg-Gly-Asp (RGD) mo...
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cell wall proteins of the ectomycorrhizal basidiomycete Pisolithus tinctorius identification function and expression in symbiosis
Fungal Genetics and Biology, 1999Co-Authors: Francis Martin, P Laurent, Catherine Voiblet, D De Carvalho, Raffaella Balestrini, Paola Bonfante, Denis TaguAbstract:Abstract Specific cell–cell and cell–substrate interactions direct the growth of ectomycorrhizal fungi to their host root targets. These elaborate mechanisms lead to the differentiation of distinct multihyphal structures, the mantle, and the Hartig net. In the ectomycorrhizal basidiomycete Pisolithus tinctorius, the use of two-dimensional gel electrophoresis, immunocytochemical microscopy, and RNA blot analysis has demonstrated the differential expression of cell wall proteins (CWPs), such as hydrophobins, adhesins, and mannoproteins, during symbiotic interaction. In other fungi, these CWPs have been suggested to play a role in hyphae aggregation, intracellular signaling cascades, and cytoskeletal changes. The recent cloning of the genes for several of these CWPs in P. tinctorius allows us to address their function in symbiosis. This review summarizes our knowledge of CWPs in P. tinctorius and considers parallels with other biotrophic fungi as a possible framework for future work.
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cloning and characterization of hydrophobins encoding cdnas from the ectomycorrhizal basidiomycete Pisolithus tinctorius
Gene, 1996Co-Authors: Denis Tagu, Birgit Nasse, Francis MartinAbstract:Abstract Major alterations of fungal gene expression are induced by the development of ectomycorrhiza, a symbiosis between tree roots and filamentous fungi. Several cDNAs corresponding to highly expressed transcripts of the Basidiomycete Pisolithus tinctorius (Pt) were isolated from symbiotic tissues. Two of these abundant transcripts ( hydPt-1 and hydPt-2 ) encoded polypeptides belonging to the hydrophobin (Hyd) family, a group of small cysteine-rich fungal proteins involved in morphogenesis and plant-fungus interactions. As shown for other Hyd, the hydPt-1 and hydPt-2 mRNAs were barely detectable in mycelium grown in liquid culture and highly accumulated in aerial hyphae. In addition, these transcripts were also abundant in Eucalyptus globulus-Pt ectomycorrhiza in early stages of differentiation, during the colonisation of roots.
J W G Cairney - One of the best experts on this subject based on the ideXlab platform.
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use of molecular methods to estimate the size and distribution of mycelial individuals of the ectomycorrhizal basidiomycete Pisolithus tinctorius
Fungal Biology, 1998Co-Authors: Ian C Anderson, Susan M Chambers, J W G CairneyAbstract:A field study was conduced to determine the size and spatial distribution of mycelial individuals of Pisolithus tinctorius at a site in NSW, Australia. Following collection and mapping of carpophores and isolation of the fungi into axenic culture, genomic DNA was extracted and combined data from RAPD and microsatellite analyses used to identify and map mycelial individuals. Thirty-three genetically distinct individuals were recognized at the field site and, while one large individual (at least 30 m diam.) was identified, most individuals appeared relatively small ( P. tinctorius mycelia through soil.
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interactions between Pisolithus tinctorius and its hosts a review of current knowledge
Mycorrhiza, 1997Co-Authors: J W G Cairney, S M ChambersAbstract:Pisolithus tinctorius (Pers.) Coker and Couch [Syn. = P. arhizus (Scop.: Pers.) Rauschert] (Pt) is a widespread ectomycorrhizal basidiomycete forming mycorrhizas with a variety of hosts. Developmental and functional aspects of the symbiosis are well documented and thus Pt has been adopted as a model organism for investigations of the molecular basis of ectomycorrhizal interactions. In this review of the current state of knowledge of interactions between Pt and its hosts we demonstrate that Pt displays much intraspecific heterogeneity of host specificity, physiology and the benefits the fungus can impart upon the host plant. It is not clear at present how far such heterogeneity reflects systematic segregation within Pt.
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efflux of phosphate from the ectomycorrhizal basidiomycete Pisolithus tinctorius general characteristics and the influence of intracellular phosphorus concentration
Fungal Biology, 1993Co-Authors: J W G Cairney, S E SmithAbstract:We have investigated phosphate absorption and efflux from mycelium of Pisolithus tinctorius and compared this with several other ecto- and ericoid mycorrhizal fungi. Phosphate absorption over a 16 h period was similar in all fungi (19–38 μmol g −1 d.w. ) with the exception of Paxillius involutus where absorption was 2–4 times greater. Efflux of phosphate from Pisolithus tinctorius followed the established pattern for efflux of ions from plant and fungal tissue. The proportion of 32 P absorbed that was lost to the bathing solution during an 8 h elution period was around 10% for all fungi. Efflux of phosphate from P. tinctorius was greatest, and absorption lowest where the fungus had a high intracellular phosphorus concentration. It is suggested that efflux of phosphate may be important in regulating mycelial phosphorus balance where mycelium has a high phosphorus status, with net efflux occurring where the intracellular orthophosphate concentration is high and the external phosphate concentration is low. The results are discussed in the context of nutrient transfer at the fungus-root interface in ectomycorrhizas.
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influence of intracellular phosphorus concentration on phosphate absorption by the ectomycorrhizal basidiomycete Pisolithus tinctorius
Fungal Biology, 1992Co-Authors: J W G Cairney, S E SmithAbstract:Mycelium of Pisolithus tinctorius grown on media with phosphate concentrations in the range 0·01–6·00 m m was found to have total phosphorus concentrations of 55–413 mol g −1 ( d.w. ) (representing 0·17–1·30% of mycelial d.w. ). The amount of phosphate absorbed by mycelium transferred to simple solutions containing orthophosphate was greatly increased in mycelium where the intracellular phosphorus concentration was 168 mol g −1 ( d.w. ) or lower. The results are discussed in relation to phosphate accumulation and translocation by the extramatrical mycelium of ectomycorrhizas in soil.
Paola Bonfante - One of the best experts on this subject based on the ideXlab platform.
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Immunolocalization of hydrophobin HYDPt‐1 from the ectomycorrhizal basidiomycete Pisolithus tinctorius during colonization of Eucalyptus globulus roots
New Phytologist, 2020Co-Authors: Denis Tagu, R De Bellis, Raffaella Balestrini, Paola Bonfante, O M H De Vries, Giovanni Piccoli, Vilberto Stocchi, F. MartinAbstract:• The immunolocalization of one of the hydrophobins of Pisolithustinctorius (HYDPt-1) is reported. Hydrophobin proteins play key roles in adhesion and aggregation of fungal hyphae, and it is already known that formation of ectomycorrhizas on eucalypt roots enhances the accumulation of hydrophobin mRNAs in the mycelium of Pisolithus tinctorius. • Purification of SDS-insoluble proteins from the mycelium of P. tinctorius showed the presence of a 13 kDa polypeptide with properties of class I hydrophobin. • Polyconal antibodies were raised against a recombinant HYDPt-1 polypeptide, and these were used for immunofluorescence-coupled transmission electron microscopy. • HYDPt-1 is a cell wall protein located at the surface of the hyphae with no preferential accumulation in the fungal cells of the different tissues of the ectomycorrhiza (i.e. extraradical hyphae, mantle or Hartig net).
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immunolocalization of hydrophobin hydpt 1 from the ectomycorrhizal basidiomycete Pisolithus tinctorius during colonization of eucalyptus globulus roots
New Phytologist, 2001Co-Authors: Denis Tagu, R De Bellis, Raffaella Balestrini, Paola Bonfante, O M H De Vries, Giovanni Piccoli, Vilberto Stocchi, F. MartinAbstract:• The immunolocalization of one of the hydrophobins of Pisolithustinctorius (HYDPt-1) is reported. Hydrophobin proteins play key roles in adhesion and aggregation of fungal hyphae, and it is already known that formation of ectomycorrhizas on eucalypt roots enhances the accumulation of hydrophobin mRNAs in the mycelium of Pisolithus tinctorius. • Purification of SDS-insoluble proteins from the mycelium of P. tinctorius showed the presence of a 13 kDa polypeptide with properties of class I hydrophobin. • Polyconal antibodies were raised against a recombinant HYDPt-1 polypeptide, and these were used for immunofluorescence-coupled transmission electron microscopy. • HYDPt-1 is a cell wall protein located at the surface of the hyphae with no preferential accumulation in the fungal cells of the different tissues of the ectomycorrhiza (i.e. extraradical hyphae, mantle or Hartig net).
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a novel class of ectomycorrhiza regulated cell wall polypeptides in Pisolithus tinctorius
Molecular Plant-microbe Interactions, 1999Co-Authors: P Laurent, Denis Tagu, Catherine Voiblet, D De Carvalho, Uwe Nehls, R De Bellis, Raffaella Balestrini, G Bauw, Paola Bonfante, F. MartinAbstract:Development of the ectomycorrhizal symbiosis leads to the aggregation of fungal hyphae to form the mantle. To identify cell surface proteins involved in this developmental step, changes in the biosynthesis of fungal cell wall proteins were examined in Eucalyptus globulus-Pisolithus tinctorius ectomycorrhizas by two-dimensional polyacrylamide gel electrophoresis. Enhanced synthesis of several immunologically related fungal 31- and 32-kDa polypeptides, so-called symbiosis-regulated acidic polypeptides (SRAPs), was observed. Peptide sequences of SRAP32d were obtained after trypsin digestion. These peptides were found in the predicted sequence of six closely related fungal cDNAs coding for ectomycorrhiza up-regulated transcripts. The PtSRAP32 cDNAs represented about 10% of the differentially expressed cDNAs in ectomycorrhiza and are predicted to encode alanine-rich proteins of 28.2 kDa. There are no sequence homologies between SRAPs and previously identified proteins, but they contain the Arg-Gly-Asp (RGD) mo...
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cell wall proteins of the ectomycorrhizal basidiomycete Pisolithus tinctorius identification function and expression in symbiosis
Fungal Genetics and Biology, 1999Co-Authors: Francis Martin, P Laurent, Catherine Voiblet, D De Carvalho, Raffaella Balestrini, Paola Bonfante, Denis TaguAbstract:Abstract Specific cell–cell and cell–substrate interactions direct the growth of ectomycorrhizal fungi to their host root targets. These elaborate mechanisms lead to the differentiation of distinct multihyphal structures, the mantle, and the Hartig net. In the ectomycorrhizal basidiomycete Pisolithus tinctorius, the use of two-dimensional gel electrophoresis, immunocytochemical microscopy, and RNA blot analysis has demonstrated the differential expression of cell wall proteins (CWPs), such as hydrophobins, adhesins, and mannoproteins, during symbiotic interaction. In other fungi, these CWPs have been suggested to play a role in hyphae aggregation, intracellular signaling cascades, and cytoskeletal changes. The recent cloning of the genes for several of these CWPs in P. tinctorius allows us to address their function in symbiosis. This review summarizes our knowledge of CWPs in P. tinctorius and considers parallels with other biotrophic fungi as a possible framework for future work.
Raffaella Balestrini - One of the best experts on this subject based on the ideXlab platform.
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Immunolocalization of hydrophobin HYDPt‐1 from the ectomycorrhizal basidiomycete Pisolithus tinctorius during colonization of Eucalyptus globulus roots
New Phytologist, 2020Co-Authors: Denis Tagu, R De Bellis, Raffaella Balestrini, Paola Bonfante, O M H De Vries, Giovanni Piccoli, Vilberto Stocchi, F. MartinAbstract:• The immunolocalization of one of the hydrophobins of Pisolithustinctorius (HYDPt-1) is reported. Hydrophobin proteins play key roles in adhesion and aggregation of fungal hyphae, and it is already known that formation of ectomycorrhizas on eucalypt roots enhances the accumulation of hydrophobin mRNAs in the mycelium of Pisolithus tinctorius. • Purification of SDS-insoluble proteins from the mycelium of P. tinctorius showed the presence of a 13 kDa polypeptide with properties of class I hydrophobin. • Polyconal antibodies were raised against a recombinant HYDPt-1 polypeptide, and these were used for immunofluorescence-coupled transmission electron microscopy. • HYDPt-1 is a cell wall protein located at the surface of the hyphae with no preferential accumulation in the fungal cells of the different tissues of the ectomycorrhiza (i.e. extraradical hyphae, mantle or Hartig net).
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immunolocalization of hydrophobin hydpt 1 from the ectomycorrhizal basidiomycete Pisolithus tinctorius during colonization of eucalyptus globulus roots
New Phytologist, 2001Co-Authors: Denis Tagu, R De Bellis, Raffaella Balestrini, Paola Bonfante, O M H De Vries, Giovanni Piccoli, Vilberto Stocchi, F. MartinAbstract:• The immunolocalization of one of the hydrophobins of Pisolithustinctorius (HYDPt-1) is reported. Hydrophobin proteins play key roles in adhesion and aggregation of fungal hyphae, and it is already known that formation of ectomycorrhizas on eucalypt roots enhances the accumulation of hydrophobin mRNAs in the mycelium of Pisolithus tinctorius. • Purification of SDS-insoluble proteins from the mycelium of P. tinctorius showed the presence of a 13 kDa polypeptide with properties of class I hydrophobin. • Polyconal antibodies were raised against a recombinant HYDPt-1 polypeptide, and these were used for immunofluorescence-coupled transmission electron microscopy. • HYDPt-1 is a cell wall protein located at the surface of the hyphae with no preferential accumulation in the fungal cells of the different tissues of the ectomycorrhiza (i.e. extraradical hyphae, mantle or Hartig net).
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a novel class of ectomycorrhiza regulated cell wall polypeptides in Pisolithus tinctorius
Molecular Plant-microbe Interactions, 1999Co-Authors: P Laurent, Denis Tagu, Catherine Voiblet, D De Carvalho, Uwe Nehls, R De Bellis, Raffaella Balestrini, G Bauw, Paola Bonfante, F. MartinAbstract:Development of the ectomycorrhizal symbiosis leads to the aggregation of fungal hyphae to form the mantle. To identify cell surface proteins involved in this developmental step, changes in the biosynthesis of fungal cell wall proteins were examined in Eucalyptus globulus-Pisolithus tinctorius ectomycorrhizas by two-dimensional polyacrylamide gel electrophoresis. Enhanced synthesis of several immunologically related fungal 31- and 32-kDa polypeptides, so-called symbiosis-regulated acidic polypeptides (SRAPs), was observed. Peptide sequences of SRAP32d were obtained after trypsin digestion. These peptides were found in the predicted sequence of six closely related fungal cDNAs coding for ectomycorrhiza up-regulated transcripts. The PtSRAP32 cDNAs represented about 10% of the differentially expressed cDNAs in ectomycorrhiza and are predicted to encode alanine-rich proteins of 28.2 kDa. There are no sequence homologies between SRAPs and previously identified proteins, but they contain the Arg-Gly-Asp (RGD) mo...
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cell wall proteins of the ectomycorrhizal basidiomycete Pisolithus tinctorius identification function and expression in symbiosis
Fungal Genetics and Biology, 1999Co-Authors: Francis Martin, P Laurent, Catherine Voiblet, D De Carvalho, Raffaella Balestrini, Paola Bonfante, Denis TaguAbstract:Abstract Specific cell–cell and cell–substrate interactions direct the growth of ectomycorrhizal fungi to their host root targets. These elaborate mechanisms lead to the differentiation of distinct multihyphal structures, the mantle, and the Hartig net. In the ectomycorrhizal basidiomycete Pisolithus tinctorius, the use of two-dimensional gel electrophoresis, immunocytochemical microscopy, and RNA blot analysis has demonstrated the differential expression of cell wall proteins (CWPs), such as hydrophobins, adhesins, and mannoproteins, during symbiotic interaction. In other fungi, these CWPs have been suggested to play a role in hyphae aggregation, intracellular signaling cascades, and cytoskeletal changes. The recent cloning of the genes for several of these CWPs in P. tinctorius allows us to address their function in symbiosis. This review summarizes our knowledge of CWPs in P. tinctorius and considers parallels with other biotrophic fungi as a possible framework for future work.