Cloning and characterization of a lectin from the octocoral Sinularia lochmodes.
In the present study, the entire amino acid sequence and cDNA structure encoding the d-galactose-binding lectin, SLL-2, isolated from the octocoral Sinularia lochmodes, were determined. SLL-2 regulates the morphology of symbiotic dinoflagellates Symbiodinium spp. through unknown mechanisms. Here, three cDNAs that encode SLL-2 were cloned and characterized. All the SLL-2 cDNAs encoded 142 amino acids with high similarity to each other. The mature subunit of SLL-2 was found to be composed of 94 amino acids and to contain one putative glycosylation site common to all three SLL-2. N-Glycopeptidase F treatment of SLL-2 resulted in a protein band shift from 16.5 to 9.5kDa in SDS-PAGE, confirming that SLL-2s are glycoproteins. Two-dimensional polyacrylamide gel electrophoresis analysis of the deglycosylated SLL-2 indicated a presence of three polypeptides as encoded in SLL-2 cDNAs. The deduced sequences of SLL-2 cDNAs had a similarity to the C-terminal region of discoidin I, the slime mold Dictyostelium discoideum lectin.
Jimbo
Mitsuru
M
Department of Marine Biosciences, School of Fisheries Sciences, Kitasato University, Oofunato, Iwate 022-0101, Japan. mjinbo@kitasato-u.ac.jp <mjinbo@kitasato-u.ac.jp>
Koike
Kazuhiko
K
Sakai
Ryuichi
R
Muramoto
Koji
K
Kamiya
Hisao
H
D000595:Amino Acid Sequence; D000818:Animals; D037421:Anthozoa / Q000737:chemistry*; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D037102:Lectins / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D018076:DNA, Complementary; D037102:Lectins