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首页> 外文期刊>Langmuir: The ACS Journal of Surfaces and Colloids >Lateral organization of a membrane protein in a supported binary lipid domain: Direct observation of the organization of bacterial light-harvesting complex 2 by total internal reflection fluorescence microscopy
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Lateral organization of a membrane protein in a supported binary lipid domain: Direct observation of the organization of bacterial light-harvesting complex 2 by total internal reflection fluorescence microscopy

机译：在支持的二元脂质结构域中膜蛋白的横向组织：通过全内反射荧光显微镜直接观察细菌捕光复合物2的组织

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摘要

A unique method is described for directly observing the lateral organization of a membrane protein ( bacterial light-harvesting complex LH2) in a supported lipid bilayer using total internal reflection fluorescence (TIRF) microscopy. The supported lipid bilayer consisted of anionic 1,2-dioleoyl-sn-glycero-3-[phospho-rac-(1)-glycerol)](DOPG) and 1,2-distearoly-sn-3-[phospho-rac-(1)-glycerol)] ( DSPG) and was formed through the rupture of a giant vesicle on a positively charged coverslip. TIRF microscopy revealed that the bilayer was composed of phase-separated domains. When a suspension of cationic phospholipid (1,2-dioleoyl-sn-glycero-3-ethylphosphocholine: EDOPC) vesicles (similar to 400 nm in diameter), containing LH2 complexes (EDOPC/LH2) 1000/1), was put into contact with the supported lipid bilayer, the cationic vesicles immediately began to fuse and did so specifically with the fluid phase (DOPG-rich domain) of the supported bilayer. Fluorescence from the incorporated LH2 complexes gradually (over similar to 20 min) spread from the domain boundary into the gel domain (DSPG-rich domain). Similar diffusion into the domain-structured supported lipid membrane was observed when the fluorescent lipid (1,2-dioleoyl-sn-glycero-3-phosphoethanolamine N- lissamine-rhodamine B sulfonyl: N- Rh-DOPE) was incorporated into the vesicles instead of LH2. These results indicate that vesicles containing LH2 and lipids preferentially fuse with the fluid domain, after which they laterally diffuse into the gel domain. This report describes for first time the lateral organization of a membrane protein, LH2, via vesicle fusion and subsequent lateral diffusion of the LH2 from the fluid to the gel domains in the supported lipid bilayer. The biological implications and applications of the present study are briefly discussed.
机译：描述了一种使用全内反射荧光（TIRF）显微镜直接观察支持的脂质双层中膜蛋白（细菌光捕获复合物LH2）的横向组织的独特方法。负载的脂质双层由阴离子1,2-二油酰基-sn-甘油-3- [磷酸-rac-（（1）-甘油）]（DOPG）和1,2-二硬脂酸-sn-3- [磷酸-rac- （1）-甘油）]（DSPG）是通过带正电的盖玻片上的巨大囊泡破裂而形成的。 TIRF显微镜显示该双层由相分离的域组成。将含有LH2络合物（EDOPC / LH2）1000/1的阳离子磷脂（1,2-油酰基-sn-甘油-3-乙基磷酸胆碱：EDOPC）囊泡（直径约400 nm）的悬浮液置于接触状态在具有支持的脂质双层的情况下，阳离子囊泡立即开始融合，并且特别是与支持的双层的液相（富含DOPG的结构域）融合。掺入的LH2复合物的荧光逐渐（约20分钟）从结构域边界扩散到凝胶结构域（富含DSPG的结构域）中。当将荧光脂质（1,2-二油酰基-sn-甘油-3-磷酸乙醇胺N-lissamine-rhodamine B磺酰基：N-Rh-DOPE）掺入囊泡中时，观察到类似的扩散到结构域支持脂质膜LH2。这些结果表明，含有LH2和脂质的囊泡优先与流体域融合，之后它们横向扩散进入凝胶域。该报告首次描述了膜蛋白LH2的横向组织，通过囊泡融合以及随后LH2从流体向支持的脂质双层中的凝胶域的横向扩散。简要讨论了本研究的生物学意义和应用。

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