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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Actin-like protein associated with plasma membranes from Euglena gracilis
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Actin-like protein associated with plasma membranes from Euglena gracilis

机译：细粒藻质膜相关的肌动蛋白样蛋白

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摘要

Microtubules are characteristic components of the membrane skeleton of Euglena gracilis, but whether microfilaments are present has been controversial. We here present evidence that an actin-like protein may indeed be associated with the plasma membrane (PM) of E. gracilis. Firstly, a 47 kDa, PM-associated, polypeptide was recognized by an anti-amoeba actin antibody. Secondly, this 47 kDa protein seemed to be peripherally attached to Phl in much the same way as P-tubulin, since both could be released from PM by treatment with 150 mM NaOH but not with ethylene glycol, NaCl, or formamide. Thirdly, the 47 kDa polypeptide and beta-tubulin were found mainly in the Triton X-114-insoluble fraction: indicating that they were part of a protein complex resistant to detergents, such as the cytoskeleton. Finally, DNase I activity was inhibited by a fraction enriched in the 47 kDa polypeptide, a property typical of actin. [References: 34]
机译：微管是Euglena gracilis膜骨架的特征成分，但是是否存在微丝一直存在争议。我们在这里提供证据，肌动蛋白样蛋白的确可能与埃希氏菌的质膜（PM）有关。首先，抗阿米巴肌动蛋白抗体识别出47 kDa与PM相关的多肽。其次，该47 kDa蛋白似乎以与P-微管蛋白几乎相同的方式附着在Phl上，因为两者均可以通过用150 mM NaOH处理而从PM中释放出来，而不是用乙二醇，NaCl或甲酰胺处理。第三，47 kDa多肽和β-微管蛋白主要存在于Triton X-114不溶级分中：表明它们是对去污剂（如细胞骨架）具有抗性的蛋白质复合物的一部分。最后，DNase I活性被富含47 kDa多肽的部分抑制，这是肌动蛋白的典型特性。 [参考：34]

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