Literature DB >> 8400136

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

M F De Bolle1, K M David, S B Rees, J Vanderleyden, B P Cammue, W F Broekaert.   

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.

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Year:  1993        PMID: 8400136     DOI: 10.1007/bf00028991

Source DB:  PubMed          Journal:  Plant Mol Biol        ISSN: 0167-4412            Impact factor:   4.076


  12 in total

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4.  Cloning and characterization of two cDNA clones encoding seed-specific antimicrobial peptides from Mirabilis jalapa L.

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Review 10.  Primary Structure Analysis of Antifungal Peptides from Cultivated and Wild Cereals.

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