Isolation and characterization of a new mannose-binding lectin gene from Taxus media.

Abstract

In this paper, we report the cloning and characterization of the first mannose-binding lectin gene from a gymnosperm plant species, Taxus media. The full-length cDNA of T. media agglutinin (TMA) consisted of 676 bp and contained a 432 bp open reading frame (ORF) encoding a 144 amino acid protein. Comparative analysis showed that TMA had high homology with many previously reported plant mannose-binding lectins and that tma encoded a precursor lectin with a 26-aa signal peptide. Molecular modelling revealed that TMA was a new mannosebinding lectin with three typical mannose-binding boxes like lectins from species of angiosperms. Tissue expression pattern analyses revealed that tma is expressed in a tissue-specific manner in leaves and stems, but not in fruits and roots. Phylogenetic tree analyses showed that TMA belonged to the structurally and evolutionarily closely related monocot mannose-binding lectin superfamily. This study provides useful information to understand the molecular evolution of plant lectins.

• Authors: Guoyin Kai, Lingxia Zhao, Jingui Zheng, Lei Zhang, Zhiqi Miao, Xiaofen Sun, Kexuan Tang
• Journal: Journal of biosciences (J Biosci) Vol. 29 Issue 4 Pg. 399-407 (Dec 2004) ISSN: 0250-5991 [Print] India
• PMID: 15625396 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• DNA, Complementary
• Mannose-Binding Lectins

Topics

• Amino Acid Sequence
• Base Sequence
• Cloning, Molecular
• DNA, Complementary (metabolism)
• Evolution, Molecular
• Mannose-Binding Lectins (genetics)
• Molecular Sequence Data
• Protein Structure, Secondary
• Protein Structure, Tertiary
• Reverse Transcriptase Polymerase Chain Reaction
• Sequence Alignment
• Taxus (genetics)