Identification and characterization of GEO1, a new class II hydrophobin from  Geosmithia  spp.
In the present paper we describe a new noncatalytic protein belonging to the hydrophobin family, designated GEO1, purified from the culture filtrate of  Geosmithia pallida  (Ascomycota: Hypocreales), and the corresponding gene sequence. In the fungal genome, GEO1 was encoded by a single-copy gene with a 450 bp open reading frame interrupted by 2 small introns whose primary translation product was 109 amino acids long and included a 23 amino acids signal peptide. The mature protein had a molecular mass of 8111.75 Da and a theoretical pI of 4.33. The deduced amino acid sequence showed similarity to class II hydrophobins and contained 8 conserved cysteine residues, present in all hydrophobins isolated so far. Biochemical properties, such as foam-forming ability and trapezoid-like shape of a GEO1 drop, also resembled the typical features of the class II hydrophobins. Expression of the geo1 gene was assessed after 2, 4, 7, 9, and 11 days of culture and showed that the geo1 transcript appeared after 7 days and increased up to 11 days.
Dipartimento di Biologia Evoluzionistica "Leo Pardi", University of Florence, via Romana 17-19, 50125 Florence, Italy. p.bettini@unifi.it
Priscilla P
PP
Bettini
Arcangela
A
Frascella
Cecilia
C
Comparini
Lara
L
Carresi
Alessia L
AL
Pepori
Luigia
L
Pazzagli
Gianni
G
Cappugi
Felice
F
Scala
Aniello
A
Scala
D000595:Amino Acid Sequence; D001483:Base Sequence; D015139:Blotting, Southern; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal; D006999:Hypocreales / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D016415:Sequence Alignment
D005656:Fungal Proteins