aspS encoding an unusual aspartyl protease from Sclerotinia sclerotiorum is expressed during phytopathogenesis.
The gene aspS encoding an aspartyl protease has been cloned from Sclerotinia sclerotiorum by screening a genomic library with a PCR-amplified fragment of the gene. The open reading frame of 1368 bp interrupted by one intron would encode a preproprotein of 435 amino acids. The catalytic aspartyl residues characteristic of aspartyl proteases are conserved; however, the active-site motif (DSG) in the N-terminal lobe is unusual in that Ser replaced Thr used in the active-site motif (DTG) of the C-terminal lobe and in all other fungal aspartyl proteases. RT-PCR revealed that aspS expression in axenic culture is not subjected to catabolite repression and demonstrated that aspS is expressed from the beginning of infection of sunflower cotyledons.
Poussereau
N
N
Laboratoire de Biologie Cellulaire Fongique [Bat. 405], ERS 2009 CNRS INSA LYON1, Microbiologie et Génétique, 43 bd 11 novembre 1918, 69622 Cedex, Villeurbanne, France
Gente
S
S
Rascle
C
C
Billon-Grand
G
G
Fèvre
M
M
D000595:Amino Acid Sequence; D001203:Ascomycota / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000472:pathogenicity*; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D001483:Base Sequence; D003470:Culture Media; D005656:Fungal Proteins; D015966:Gene Expression Regulation, Fungal; D006368:Helianthus / Q000382:microbiology*; D008969:Molecular Sequence Data; D010935:Plant Diseases / Q000382:microbiology; D017422:Sequence Analysis, DNA; D014774:Virulence
D003470:Culture Media; D005656:Fungal Proteins; D016282:Aspartic Acid Endopeptidases; C427243:aspartyl protease, Sclerotinia sclerotiorum