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.
De Bolle
M F
MF
F.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee, Belgium.
David
K M
KM
Rees
S B
SB
Vanderleyden
J
J
Cammue
B P
BP
Broekaert
W F
WF
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