F. Shao et al., A new antifungal peptide from the seeds of Phytolacca americana: characterization, amino acid sequence and cDNA cloning, BBA-PROT ST, 1430(2), 1999, pp. 262-268
Citations number
21
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
An antifungal peptide from seeds of Phytolacca americana, designated PAFP-s
, has been isolated. The peptide is highly basic and consists of 38 residue
s with three disulfide bridges. Its molecular mass of 3929.0 was determined
by mass spectrometry. The complete amino acid sequence was obtained from a
utomated Edman degradation, and cDNA cloning was successfully performed by
3'-RACE. The deduced amino acid sequence of a partial cDNA corresponded to
the amino acid sequence from chemical sequencing. PAFP-s exhibited a broad
spectrum of antifungal activity, and its activities differed among various
fungi. PAFP-s displayed no inhibitory activity towards Escherichia coli. PA
FP-s shows significant sequence similarities and the same cysteine motif wi
th Mj-AMPs, antimicrobial peptides from seeds of Mirabilis jalapa belonging
to the knottin-type antimicrobial peptide. (C) 1999 Elsevier Science B.V.
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