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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Evolution and adaptation of single-pass transmembrane proteins
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Evolution and adaptation of single-pass transmembrane proteins

机译：单通跨膜蛋白的进化与适应

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Abstract A comparative analysis of 6039 single-pass (bitopic) membrane proteins from six evolutionarily distant organisms was performed based on data from the Membranome database. The observed repertoire of bitopic proteins is significantly enlarged in eukaryotic cells and especially in multicellular organisms due to the diversification of enzymes, emergence of proteins involved in vesicular trafficking, and expansion of receptors, structural, and adhesion proteins. The majority of bitopic proteins in multicellular organisms are located in the plasma membrane (PM) and involved in cell communication. Bitopic proteins from different membranes significantly diverge in terms of their biological functions, size, topology, domain architecture, physical properties of transmembrane (TM) helices and propensity to form homodimers. Most proteins from eukaryotic PM and endoplasmic reticulum (ER) have the N-out topology. The predicted lengths of TM helices and hydrophobic thicknesses, stabilities and hydrophobicities of TM α-helices are the highest for proteins from eukaryotic PM, intermediate for proteins from prokaryotic cells, ER and Golgi apparatus, and lowest for proteins from mitochondria, chloroplasts, and peroxisomes. Tyr and Phe residues accumulate at the cytoplasmic leaflet of PM and at the outer leaflet of membranes of bacteria, Golgi apparatus, and nucleus. The propensity for dimerization increases from unicellular to multicellular eukaryotes, from enzymes to receptors, and from intracellular membrane proteins to PM proteins. More than half of PM proteins form homodimers with a 2:1 ratio of right-handed to left-handed helix packing arrangements. The inverse ratio (1:2) was observed for dimers from the ER, Golgi and vesicles. Graphical abstract Display Omitted Highlights ? Sizes, topologies, localizations, and functions of bitopic proteins were analyzed. ? Physical properties of TM helices of bitopic proteins of 6 organisms were compared. ? TM segment length, thickness, stability and hydrophobicity are organelle-specific. ? Computational models of 2129 TM α-helical homodimers were analyzed. ? Dimerization propensity is higher for receptors of multicellular organisms.
机译：摘要基于来自膜组态数据库的数据进行6039单通（Bitopic）膜蛋白的对比分析。观察到的Bitopic蛋白在真核细胞中显着扩大，特别是由于酶的多样化，特别是蛋白质的出现，以及受体，结构和粘附蛋白的膨胀，蛋白质的出现。多细胞生物体中的大多数Bitopic蛋白位于血浆膜（PM）中并参与细胞连通。在不同膜的Bitopic蛋白在其生物学功能，大小，拓扑，域架构，跨膜（TM）螺旋的物理性质和形成同型二聚体的倾向方面显着发散。来自真核蛋白PM和内质网（ER）的大多数蛋白质具有N-OUT拓扑。 TMα-螺旋的TM螺旋和疏水性厚度，稳定性和疏水性的预测长度是来自真核生物PM的蛋白质的最高蛋白质，来自原核细胞，ER和GOLGI装置的蛋白质中间体，以及来自线粒体，叶绿体和过氧磷酸的蛋白质最低的蛋白质。 Tyr和Phe残基在PM的细胞质传单中积聚在细菌，GOLGI装置和核的膜外瓣叶上。二聚化的倾向从单细胞到多细胞真核生物增加，从酶到受体，从细胞内膜蛋白到PM蛋白质。超过一半的PM蛋白质形成同型二聚体的右手与左手螺旋填料布置的2：1的比例。从ER，GOLGI和囊泡的二聚体观察到逆比（1：2）。图形抽象显示省略了亮点？分析了Bitopic蛋白的尺寸，拓扑，本地化和功能。还比较了6个生物的Bitopic蛋白的TM螺旋的物理性质。还TM段长度，厚度，稳定性和疏水性是细胞器特异性的。还分析了2129吨α-螺旋同型二聚体的计算模型。还对于多细胞生物体的受体来说，二聚化倾向更高。

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