Cloning and characterization of a cDNA encoding an antimicrobial chitin-binding protein from amaranth, Amaranthus caudatus.
A cDNA clone encoding an antimicrobial chitin-binding protein from amaranth (Amaranthus caudatus L.) was isolated using a cDNA library constructed from near-mature seed poly(A)+ mRNA. The deduced amino acid sequence of the cDNA clone encodes a predicted polypeptide of 86 amino acids. This polypeptide has three distinct domains: an amino-terminal putative signal peptide (25 amino acids), a domain corresponding to the mature protein (30 amino acids), and a carboxyl-terminal propeptide (31 amino acids) containing a putative N-glycosylation site. The encoded protein differs from all known members of the family of chitin-binding proteins. Transcripts of the expected size (650 bp) are present in developing seeds but not in roots, leaves or stressed leaves.
F.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee, Belgium.
M F
MF
De Bolle
K M
KM
David
S B
SB
Rees
J
J
Vanderleyden
B P
BP
Cammue
W F
WF
Broekaert
D000595:Amino Acid Sequence; D000890:Anti-Infective Agents; D001483:Base Sequence; D015152:Blotting, Northern; D002686:Chitin / Q000378:metabolism*; D003001:Cloning, Molecular; D004247:DNA; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000235:genetics* / Q000378:metabolism; D010944:Plants / Q000235:genetics*
D000890:Anti-Infective Agents; D010940:Plant Proteins; C074242:AMP2 protein, Amaranthus caudatus; D002686:Chitin; D004247:DNA