Cloning and characterization of a cDNA encoding an antimicrobial chitin-binding protein from amaranth, Amaranthus caudatus

Plant Mol Biol. 1993 Sep;22(6):1187-90. doi: 10.1007/BF00028991.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Infective Agents*
  • Base Sequence
  • Blotting, Northern
  • Chitin / metabolism*
  • Cloning, Molecular
  • DNA
  • Molecular Sequence Data
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism
  • Plants / genetics*

Substances

  • Anti-Infective Agents
  • Plant Proteins
  • AMP2 protein, Amaranthus caudatus
  • Chitin
  • DNA