EglD, a putative endoglucanase, with an expansin like domain is localized in the conidial cell wall of Aspergillus nidulans

Bouzarelou, Demetra; Billini, Maria; Roumelioti, Katerina; Sophianopoulou, Vicky

doi:10.1016/j.fgb.2008.03.001

Cited by 30 publications

(23 citation statements)

References 73 publications

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“…However, expansin-like proteins have also been found in fungi and bacteria (often called swollenins or loosenins) (Bouzarelou et al 2008;Brotman et al 2008;Chen et al 2010;Dermatsev et al 2010;Kerff et al 2008;Lee et al 2010;Quiroz-Castañeda et al 2011;Saloheimo et al 2002;Yao et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Cerato-platanin shows expansin-like activity on cellulosic materials

Baccelli

Luti

Bernardi

et al. 2013

Appl Microbiol Biotechnol

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Cerato-platanin (CP) is a non-catalytic protein with a double =β-barrel fold located in the cell wall of the phytopathogenic fungus Ceratocystis platani. CP is released during growth and induces defence-related responses in plants. CP is also the first member of the "cerato-platanin family" (CPF) (Pfam PF07249). In the CPF, the molecular mechanism of action on plants and above all the biological role in fungal life are little-known aspects. However, an expansin-like function has recently been suggested concerning CP. Expansin-like proteins have the ability to act non-hydrolytically on cellulose. In the present work, the expansin-like activity of CP and Pop1, a CP family member, was investigated. Like expansins, CP and Pop1 were able to weaken filter paper in a concentration-dependent manner and without the production of reducing sugars. A metal-dependent polysaccharide monooxygenase-like activity was excluded. The optimum of activity was pH5.0, 38°C. CP was also able to cause fragmentation of the crystalline cellulose Avicel and the breakage and defibration of cotton fibres. However, the interaction did not involve a stable bond with the substrates and CP did not significantly enhance the hydrolytic activity of cellulase. On the other hand, CP and Pop1 bound quickly to chitin. We consider CP as a novel one-domain expansin-like protein. We propose a structural role for CP in the fungal cell wall due to the ability to bind chitin, and hypothesize a functional role in the interaction of the fungus with the plant for the weakening activity shown on cellulose.

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Section: Introductionmentioning

confidence: 99%

Cerato-platanin shows expansin-like activity on cellulosic materials

Baccelli

Luti

Bernardi

et al. 2013

Appl Microbiol Biotechnol

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“…CELL tion remains baffling. EglD, a putative endoglucanase comprising an expansin-like domain, also localizes at the periphery of ungerminated conidia (7). It would be of interest to study whether this localization implies a topological or functional association with eisosomes.…”

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confidence: 99%

Eisosome Organization in the Filamentous AscomyceteAspergillus nidulans

et al. 2010

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Eisosomes are subcortical organelles implicated in endocytosis and have hitherto been described only in Saccharomyces cerevisiae. They comprise two homologue proteins, Pil1 and Lsp1, which colocalize with the transmembrane protein Sur7. These proteins are universally conserved in the ascomycetes. We identify in Aspergillus nidulans (and in all members of the subphylum Pezizomycotina) two homologues of Pil1/Lsp1, PilA and PilB, originating from a duplication independent from that extant in the subphylum Saccharomycotina. In the aspergilli there are several Sur7-like proteins in each species, including one strict Sur7 orthologue (SurG in A. nidulans). In A. nidulans conidiospores, but not in hyphae, the three proteins colocalize at the cell cortex and form tightly packed punctate structures that appear different from the clearly distinct eisosome patches observed in S. cerevisiae. These structures are assembled late during the maturation of conidia. In mycelia, punctate structures are present, but they are composed only of PilA, while PilB is diffused in the cytoplasm and SurG is located in vacuoles and endosomes. Deletion of each of the genes does not lead to any obvious growth phenotype, except for moderate resistance to itraconazole. We could not find any obvious association between mycelial (PilA) eisosome-like structures and endocytosis. PilA and SurG are necessary for conidial eisosome organization in ways that differ from those for their S. cerevisiae homologues. These data illustrate that conservation of eisosomal proteins within the ascomycetes is accompanied by a striking functional divergence.

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“…Expansins are involved in cell wall loosening during plant cell growth by disrupting hydrogen bonding between cellulose microfibrils and thereby allowing the sliding of cellulose fibers. Expansins were also found in bacteria and fungi (Bouzarelou et al, 2008;Martin et al, 2008;Kerff et al, 2008). Addition of the Bacillus subtilis expansin BsEXLX1 to an industrial cellulase cocktail led to a 2.6-fold increase in sugar yield upon hydrolysis of filter paper (Kim et al, 2009).…”

Section: Supplementation Of T Reesei Cellulase Cocktails With Non-hymentioning

confidence: 99%