Publication: Identification and characterization of a novel legume-like lectin cDNA sequence from the red marine algae Gracilaria fisheri
Issued Date
2011-12-01
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ISSN
09737138
02505991
02505991
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2-s2.0-84858720130
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Biosciences. Vol.36, No.5 (2011), 833-843
Suggested Citation
Sukanya Suttisrisung, Saengchan Senapin, Boonsirm Withyachumnarnkul, Kanokpan Wongprasert Identification and characterization of a novel legume-like lectin cDNA sequence from the red marine algae Gracilaria fisheri. Journal of Biosciences. Vol.36, No.5 (2011), 833-843. doi:10.1007/s12038-011-9144-8 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/11229
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Title
Identification and characterization of a novel legume-like lectin cDNA sequence from the red marine algae Gracilaria fisheri
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Abstract
A legume-type lectin (L-lectin) gene of the red algae Gracilaria fisheri (GFL) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA of GFL was 1714 bp and contained a 1542 bp open reading frame encoding 513 amino acids with a predicted molecular mass of 56.5 kDa. Analysis of the putative amino acid sequence with NCBI-BLAST revealed a high homology (30-68%) with legume-type lectins (L-lectin) from Griffithsia japonica, Clavispora lusitaniae, Acyrthosiphon pisum, Tetraodon nigroviridis and Xenopus tropicalis. Phylogenetic relationship analysis showed the highest sequence identity to a glycoprotein of the red algae Griffithsia japonica (68%) (GenBank number AAM93989). Conserved Domain Database analysis detected an N-terminal carbohydrate recognition domain (CRD), the characteristic of L-lectins, which contained two sugar binding sites and a metal binding site. The secondary structure prediction of GFL showed a β-sheet structure, connected with turn and coil. The most abundant structural element of GFL was the random coil, while the α-helixes were distributed at the N- and C-termini, and 21 β-sheets were distributed in the CRD. Computer analysis of three-dimensional structure showed a common feature of L-lectins of GFL, which included an overall globular shape that was composed of a β-sandwich of two anti-parallel β-sheets, monosaccharide binding sites, were on the top of the structure and in proximity with a metal binding site. Northern blot analysis using a DIG-labelled probe derived from a partial GFL sequence revealed a hybridization signal of ∼1.7 kb consistent with the length of the full-length GFL cDNA identified by RACE. No detectable band was observed from control total RNA extracted from filamentous green algae. © Indian Academy of Sciences.