cDNA cloning and characterization of a mannose-binding lectin from Zingiber officinale Roscoe (ginger) rhizomes.
J Biosci
;
2005 Mar; 30(2): 213-20
Article
in English
| IMSEAR
| ID: sea-111342
ABSTRACT
Using RNA extracted from Zingiber officinale rhizomes and primers designed according to the conservative regions of monocot mannose-binding lectins, the full-length cDNA of Z. officinale agglutinin (ZOA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA of zoa was 746 bp and contained a 510 bp open reading frame (ORF) encoding a lectin precursor of 169 amino acids with a signal peptide. ZOA was a mannose-binding lectin with three typical mannose-binding sites (QDNY). Semi-quantitative RT-PCR analysis revealed that zoa expressed in all the tested tissues of Z. officinale including leaf, root and rhizome, suggesting it to be a constitutively expressing form. ZOA protein was successfully expressed in Escherichia coli with the molecular weight expected. To our knowledge, this is the first mannose-binding lectin cDNA cloned from the family Zingiberaceae. Our results demonstrate that monocot mannose-binding lectins also occur within the family Zingiberaceae.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Phylogeny
/
Binding Sites
/
Molecular Sequence Data
/
Base Sequence
/
Cluster Analysis
/
Gene Expression
/
Amino Acid Sequence
/
Cloning, Molecular
/
Sequence Analysis, DNA
/
DNA, Complementary
Language:
English
Journal:
J Biosci
Year:
2005
Type:
Article
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