MOLECULAR CHARACTERIZATION OF THE LECTIN, BRYOHEALIN, INVOLVED IN PROTOPLAST REGENERATION OF THE MARINE ALGA BRYOPSIS PLUMOSA (CHLOROPHYTA)(1)

© 2008 Phycological Society of America.

Bibliographische Detailangaben
Veröffentlicht in:Journal of phycology. - 1966. - 44(2008), 1 vom: 25. Feb., Seite 103-12
1. Verfasser: Yoon, Kang Sup (VerfasserIn)
Weitere Verfasser: Lee, Key Pyoung, Klochkova, Tatyana A, Kim, Gwang Hoon
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2008
Zugriff auf das übergeordnete Werk:Journal of phycology
Schlagworte:Journal Article Bryohealin Bryopsis plumosa green algae lectin protoplast formation recombinant
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520 |a When a coenocytic cell of the green alga Bryopsis plumosa (Hudson) C. Agardh was cut open and the cell contents expelled, the cell organelles agglutinated rapidly in seawater to form protoplasts. This process was mediated by a lectin, Bryohealin. The full sequence of the cDNA encoding Bryohealin was obtained, which consisted of 1,101 base pairs (bp), with 24 bp of 5' untranslated region (UTR) and 201 bp of 3' UTR. It had an open reading frame (ORF) of 771 bp encoding 257 amino acid residues. A signal peptide consisted of 22 amino acids presented before the start codon of Bryohealin, indicating that this lectin was a vacuolar (storage) protein. The C-terminal sequence of Bryohealin was composed of antibiotic domains, suggesting that this lectin could perform two functions: (i) aggregation of cell organelles in seawater and (ii) protection from bacterial contamination for successful protoplast regeneration. The BLAST search result showed that Bryohealin had little sequence homology with any known plant lectins, but rather resembled animal lectins with fucolectin domains. The expression of recombinant Bryohealin (rBryohealin) was obtained in the Escherichia coli system 
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700 1 |a Lee, Key Pyoung  |e verfasserin  |4 aut 
700 1 |a Klochkova, Tatyana A  |e verfasserin  |4 aut 
700 1 |a Kim, Gwang Hoon  |e verfasserin  |4 aut 
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