Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 404-414 |
| Seitenumfang | 11 |
| Fachzeitschrift | Journal of basic microbiology |
| Jahrgang | 51 |
| Ausgabenummer | 4 |
| Publikationsstatus | Veröffentlicht - 24 März 2011 |
Abstract
The entomopathogenic ascomycete Paecilomyces farinosus (alternative name Isaria farinosa) synthesized a hydrophobin, irrespective of being grown in submerged or surface culture. The protein was extracted using trifluoroacetic acid and purified using preparative HPLC and SDS-PAGE. Partial sequences were obtained using ESI-MS/MS. The peptides were used as a start to apply a 'template switching oligo' protocol to elucidate the complete open reading frame of P. farinosus hydrophobin 1 (pfah1). The deduced protein sequence comprised 107 amino acids (10.7 kDa) including a 16 amino acid long hydrophobic signal peptide, showed a calculated pI of 4.56, and was interrupted by one intron. Phylogenetic analyses revealed relationships to hydrophobins of the ascomycetes Magnaporthe grisea and Metarhizium anisopliae. Based on solubility, hydropathy pattern and phylogeny PfaH1 was assigned to the class Ia hydrophobins.
ASJC Scopus Sachgebiete
- Immunologie und Mikrobiologie (insg.)
- Angewandte Mikrobiologie und Biotechnologie
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in: Journal of basic microbiology, Jahrgang 51, Nr. 4, 24.03.2011, S. 404-414.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Characterization of a hydrophobin of the ascomycete Paecilomyces farinosus
AU - Lunkenbein, Stefan
AU - Takenberg, Meike
AU - Nimtz, Manfred
AU - Berger, Ralf G.
PY - 2011/3/24
Y1 - 2011/3/24
N2 - The entomopathogenic ascomycete Paecilomyces farinosus (alternative name Isaria farinosa) synthesized a hydrophobin, irrespective of being grown in submerged or surface culture. The protein was extracted using trifluoroacetic acid and purified using preparative HPLC and SDS-PAGE. Partial sequences were obtained using ESI-MS/MS. The peptides were used as a start to apply a 'template switching oligo' protocol to elucidate the complete open reading frame of P. farinosus hydrophobin 1 (pfah1). The deduced protein sequence comprised 107 amino acids (10.7 kDa) including a 16 amino acid long hydrophobic signal peptide, showed a calculated pI of 4.56, and was interrupted by one intron. Phylogenetic analyses revealed relationships to hydrophobins of the ascomycetes Magnaporthe grisea and Metarhizium anisopliae. Based on solubility, hydropathy pattern and phylogeny PfaH1 was assigned to the class Ia hydrophobins.
AB - The entomopathogenic ascomycete Paecilomyces farinosus (alternative name Isaria farinosa) synthesized a hydrophobin, irrespective of being grown in submerged or surface culture. The protein was extracted using trifluoroacetic acid and purified using preparative HPLC and SDS-PAGE. Partial sequences were obtained using ESI-MS/MS. The peptides were used as a start to apply a 'template switching oligo' protocol to elucidate the complete open reading frame of P. farinosus hydrophobin 1 (pfah1). The deduced protein sequence comprised 107 amino acids (10.7 kDa) including a 16 amino acid long hydrophobic signal peptide, showed a calculated pI of 4.56, and was interrupted by one intron. Phylogenetic analyses revealed relationships to hydrophobins of the ascomycetes Magnaporthe grisea and Metarhizium anisopliae. Based on solubility, hydropathy pattern and phylogeny PfaH1 was assigned to the class Ia hydrophobins.
KW - Ascomycete
KW - Fungi
KW - Hydrophobin
KW - Paecilomyces farinosus
UR - http://www.scopus.com/inward/record.url?scp=79961199224&partnerID=8YFLogxK
U2 - 10.1002/jobm.201000305
DO - 10.1002/jobm.201000305
M3 - Article
C2 - 21656798
AN - SCOPUS:79961199224
VL - 51
SP - 404
EP - 414
JO - Journal of basic microbiology
JF - Journal of basic microbiology
SN - 0233-111X
IS - 4
ER -