The thn mutation of Schizophyllum commune, which suppresses formation of aerial hyphae, affects expression of the Sc3 hydrophobin gene

Wessels, J. G. H.; Vries, O.; Ásgeirsdóttir, Sigrídur A.; Springer, Jan

doi:10.1099/00221287-137-10-2439

Cited by 127 publications

(83 citation statements)

References 23 publications

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“…The 14.5-kDa protein, HsbA, can bind to PBSA and recruit cutinase CutL1. HsbA does not contain any cysteine residues, so it is not formally classifiable as a hydrophobin (3,31,32). Genes orthologous or paralogous to hsbA in other fungi are known (EAL94060, EAL84331, EAA58613, and AAB69331), but none of the orthologues have been functionally characterized.…”

Section: Discussionmentioning

confidence: 99%

Novel Hydrophobic Surface Binding Protein, HsbA, Produced by Aspergillus oryzae

Ohtaki

Maéda

Takahashi

et al. 2006

Appl Environ Microbiol

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Hydrophobic surface binding protein A (HsbA) is a secreted protein (14.5 kDa) isolated from the culture broth of Aspergillus oryzae RIB40 grown in a medium containing polybutylene succinate-co-adipate (PBSA) as a sole carbon source. We purified HsbA from the culture broth and determined its N-terminal amino acid sequence. We found a DNA sequence encoding a protein whose N terminus matched that of purified HsbA in the A. ozyzae genomic sequence. We cloned the hsbA genomic DNA and cDNA from A. oryzae and constructed a recombinant A. oryzae strain highly expressing hsbA. Orthologues of HsbA were present in animal pathogenic and entomopathogenic fungi. Heterologously synthesized HsbA was purified and biochemically characterized. Although the HsbA amino acid sequence suggests that HsbA may be hydrophilic, HsbA adsorbed to hydrophobic PBSA surfaces in the presence of NaCl or CaCl 2 . When HsbA was adsorbed on the hydrophobic PBSA surfaces, it promoted PBSA degradation via the CutL1 polyesterase. CutL1 interacts directly with HsbA attached to the hydrophobic QCM electrode surface. These results suggest that when HsbA is adsorbed onto the PBSA surface, it recruits CutL1, and that when CutL1 is accumulated on the PBSA surface, it stimulates PBSA degradation. We previously reported that when the A. oryzae hydrophobin RolA is bound to PBSA surfaces, it too specifically recruits CutL1. Since HsbA is not a hydrophobin, A. oryzae may use several types of proteins to recruit lytic enzymes to the surface of hydrophobic solid materials and promote their degradation.

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Section: Discussionmentioning

confidence: 99%

Novel Hydrophobic Surface Binding Protein, HsbA, Produced by Aspergillus oryzae

Ohtaki

Maéda

Takahashi

et al. 2006

Appl Environ Microbiol

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“…The Sc3p of S. commune aggregates on the aerial hyphae as SDS-insoluble complexes (Wessels et al, 1991 a), and cryparin and cerato-ulmin have been shown to be present in the cell walls of aerial hyphae of C. purusitica and 0. ulrni, respectively, by immunofluorescent microscopy (Carpenter et al, 1992) and immunoelectron microscopy (Svircev et al, 1988). S. commune Sc3p has been shown to be secreted from the tips of the submerged hyphae (Wosten et al, 1994a) but the cell walls of submerged hyphae, however, were reported to lack Sc3p.…”

Section: Discussionmentioning

confidence: 99%

“…Hydrophobic amino acids are shown below and hydrophilic amino acids above the x-axis. The amino acids of the hydrophobins, including the signal sequences, are shown along the x-axis like protcins were searched for by comparing the properties of a protein with those described for hydrophobins (Wessels et al, 1991 a ;Wosten el al., 1993;Carpenter et al, 1992). To verify if one of the hydrophobin-like proteins was HFBI, the hjb/ gene was cxpressed in E. coli as a FLAG fusion (see Experimental Procedures), and antibodies were prepared against the fusion protein (Fig.…”

Section: Localization Of the Hfbi Proteinmentioning

confidence: 99%

Genetic and Biochemical Characterization of the Trichoderma Reesei Hydrophobin HFBI

Nakari-Setälä¹,

Aro²,

Kalkkinen

et al. 1996

European Journal of Biochemistry

102

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The hjbl gene of the filamentous fungus Trichodermu reesei, previously cloned as a gene which was abundantly expressed when the fungus was grown on glucose-containing medium, was shown to encode a novel fungal hydrophobin. The encoded 97-amino-acid protein is cysteine-rich and has a typical signal sequence for secretion. Signal-sequence cleavage and putative proteolytic processing results in the mature HFBI protein of 75 amino acids. Antibodies raised against the HFBI protein expressed in Escherichiu coli detected the 7: reesei HFBI protein in the fungal cell wall and in the culture medium of submerged glucose-containing cultures. The identity of HFBI was verified by N-terminal and peptide sequencing or proteins purified both from the cell wall and culture medium. In the cell wall most of the HFBI rormed SDS-insoluble complexes that could be extracted with trifluoroacetic acid. Bubbling or freezing of the culture medium caused HFBI to form aggregates that coprecipitated with a yellow pigment produced by the fungus.

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“…Other potential components include cysteinerich, ca. 30-kDa "hydrophobins" which have been isolated from the outer surface of Schizophyllum commune and Aspergillus nidulans (41,42) but have yet to be identified or characterized in C albicans.…”

Section: Discussionmentioning

confidence: 99%

Isolation of a Candida albicans DNA sequence conferring adhesion and aggregation on Saccharomyces cerevisiae

Barki¹,

Koltin²,

Yanko³

et al. 1993

J Bacteriol

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Candida albicans is an opportunistic pathogen which may give rise to superficial and systemic infections. In the present study, C. albicans adhesion was studied by expression of C. albicans DNA sequences encoding adhesion functions in a nonadherent strain of Saccharomyces cerevisiae. Adherent transformant cells of S. cerevisiae harbouring a C. albicans genomic library cloned in a yeast-Escherichia coli shuttle vector were selected by using tissue culture-treated polystyrene as the attachment substratum. One transformant exhibited enhanced adhesion to treated and untreated polystyrene as well as autoaggregation, unlike control cells bearing the vector alone. Analysis of this clone revealed an insert of ca. 4.5 kb from C. albicans. Curing of the plasmid resulted in loss of adhesion and autoaggregation properties. A subclone bearing a reduced insert of 3.3 kb retained the ability to autoaggregate, to bind to treated and untreated polystyrene, and to adhere to buccal epithelial cells, unlike appropriate controls. Further subcloning of the insert to 2.7- and 1.9-kb fragments resulted in incremental decreases in adhesion and autoaggregation, whereas smaller fragments did not confer these properties. Hybridization of the 2.7-kb segment with C. albicans and S. cerevisiae DNA confirmed its origin as a single-copy sequence in the C. albicans genome as well as the absence of a homologous sequence in the genome of S. cerevisiae. The data suggest that the adhesion and aggregation phenomena of the transformant cells are related to expression of a C. albicans surface antigen encoded by the cloned DNA fragment.

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The thn mutation of Schizophyllum commune, which suppresses formation of aerial hyphae, affects expression of the Sc3 hydrophobin gene

Cited by 127 publications

References 23 publications

Novel Hydrophobic Surface Binding Protein, HsbA, Produced by Aspergillus oryzae

Novel Hydrophobic Surface Binding Protein, HsbA, Produced by Aspergillus oryzae

Genetic and Biochemical Characterization of the Trichoderma Reesei Hydrophobin HFBI

Isolation of a Candida albicans DNA sequence conferring adhesion and aggregation on Saccharomyces cerevisiae

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