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Tuning a bacterial chemoreceptor with protein-membrane interactions

机译：通过蛋白膜相互作用调节细菌化学感受器

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摘要

Chemoreceptors in Escherichia coli are homodimeric transmembrane proteins that convert environmental stimuli into intracellular signals controlling flagellar motion. Chemoeffectors bind to the extracellular (periplasmic) domain of the receptors, whereas their cytoplasmic domain mediates signaling and adaptation. The second transmembrane helix (TM2) connects these two domains. TM2 contains an aliphatic core flanked by amphipathic aromatic residues that have specific affinity for polar-hydrophobic membrane interfaces. We previously showed that Trp-209, near the cytoplasmic end of TM2, helps maintain the normal baseline-signaling state of the aspartate chemoreceptor (Tar) and that Tyr-210 plays an auxiliary role in this control. We have now repositioned the Trp-209/Tyr-210 pair in single-residue increments about the cytoplasmic polar-hydrophobic interface. Changes from WY-2 to WY+1 modulate the baseline-signaling state of the receptor in predictable and incremental steps that can be compensated by adaptive methylation/demethylation. Greater displacements, as in WY-3, WY+2, and WY+3, bias the receptor to the off kinase-inhibiting state or the on kinase-stimulating state, respectively, to a degree that cannot be fully compensated by the adaptation system. Aromatic residues analogous to Trp-209/Tyr-210 are present in other chemoreceptors and many transmembrane sensor kinases, where they may serve a similar function.
机译：大肠杆菌中的化学感受器是同二聚体跨膜蛋白，可将环境刺激转换为控制鞭毛运动的细胞内信号。化学效应子与受体的胞外（周质）域结合，而它们的胞质域介导信号传导和适应。第二个跨膜螺旋（TM2）连接这两个域。 TM2包含一个脂族核心，其侧翼是两亲性芳香族残基，该残基对极性疏水膜的界面具有特定的亲和力。我们先前显示，TM2胞质末端附近的Trp-209可帮助维持天冬氨酸化学感受器（Tar）的正常基线信号状态，而Tyr-210在此控制中起辅助作用。现在，我们以关于细胞质极性-疏水性界面的单残基增量重新定位了Trp-209 / Tyr-210对。从WY-2到WY + 1的变化以可预测和增量的方式调节受体的基线信号状态，可以通过适应性甲基化/去甲基化来补偿。在WY-3，WY + 2和WY + 3中，更大的位移分别将受体偏向关闭激酶抑制状态或开启激酶刺激状态，达到无法由适应系统完全补偿的程度。在其他化学感受器和许多跨膜传感器激酶中也存在类似于Trp-209 / Tyr-210的芳香族残基，它们在其中可能起着类似的作用。

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