Characterization of a new lectin involved in the protoplast regeneration of Bryopsis hypnoides
Characterization of a new lectin involved in the protoplast regeneration of Bryopsis hypnoides
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DOI:
10.1007/s00343-009-9157-4
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发表时间:
2009-11
影响因子:
--
通讯作者:
J. Niu;Guangce Wang;F. Lü;Bai-cheng Zhou;G. Peng
中科院分区:
文献类型:
--
作者:
J. Niu;Guangce Wang;F. Lü;Bai-cheng Zhou;G. Peng
A group of coenocytic marine algae differs from higher plants, whose totipotency depends on an intact cell (or protoplast). Instead, this alga is able to aggregate its extruded protoplasm in sea water and generate new mature individuals. It is thought that lectins play a key role in the aggregation process. We purified a lectin associated with the aggregation of cell organelles in Bryopsis hypnoides. The lectin was ca. 27 kDa with a pI between pH 5 and pH 6. The absence of carbohydrate suggested that the lectin was not a glycoprotein. The hemagglutinating activity (HA) of the lectin was not dependent on the presence of divalent cations and was inhibited by N-Acetylgalactosamine, N-Acetylglucosamine, and the glycoprotein bovine submaxillary mucin. The lectin preferentially agglutinated Gram-negative bacterium. The HA of this lectin was stable between pH 4 to pH 10. Cell organelles outside the cytoplasm were agglutinated by the addition of lectin solution (0.5 mg ml−1). Our results suggest that the regeneration of B. hypnoides is mediated by this lectin. We also demonstrated that the formation of cell organelle aggregates was inhibited by nigericin in natural seawater (pH 8.0). Given that nigericin dissipates proton gradients across the membrane, we hypothesize that the aggregation of cell organelles was proton-gradient dependent.