Structure and dynamics of the central lipid pool and protein components of the bacterial holo-translocon

Structure and dynamics of the central lipid pool and protein components of the bacterial holo-translocon
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细菌全息子的中心脂质池和蛋白质成分的结构和动力学

DOI:
10.1101/490250
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发表时间:
2018
期刊:
--
影响因子:
--
通讯作者:
Martin R
Martin R
中科院分区:
--
文献类型:
--
作者:
Martin R

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细菌 Sec 易位子 SecYEG 与辅助蛋白 YidC 和 SecDF-YajC 子复合体结合形成细菌全息位子 (HTL)。 HTL 是一种动态且灵活的蛋白质转运机器,能够协调跨膜蛋白质分泌,以及新生膜蛋白质的有效横向插入。据推测,中央脂质核心有助于膜蛋白受控进入双层,确保其天然状态的有效形成。通过对溶解在匹配的氘化去污剂中的蛋白质进行小角中子散射 (SANS),我们已经能够询问“裸”HTL 复合物,而周围去污剂胶束的散射贡献变得不可见。这种方法可以确认 HTL 内的脂质核心,该核心可容纳 8 至 29 种脂质。 HTL 的粗粒度分子动力学模拟还展示了动态的中心脂质池。 YidC 和 SecY 侧门之间的富含脂质区域的开口可能为新合成的、正确定向的膜蛋白螺旋从 HTL 中出现提供出口。
The bacterial Sec translocon, SecYEG, associates with accessory proteins YidC and the SecDF-YajC subcomplex to form the bacterial holo-translocon (HTL). The HTL is a dynamic and flexible protein transport machine capable of coordinating protein secretion across the membrane, and efficient lateral insertion of nascent membrane proteins. It has been hypothesized that a central lipid core facilitates the controlled passage of membrane proteins into the bilayer, ensuring efficient formation of their native state. By performing small-angle neutron scattering (SANS) on protein solubilized in match-out deuterated detergent, we have been able to interrogate a ‘naked’ HTL complex, with the scattering contribution of the surrounding detergent micelle rendered invisible. Such an approach has allowed the confirmation of a lipid core within the HTL, which accommodates between 8 and 29 lipids. Coarse-grained molecular dynamics simulations of the HTL also demonstrate a dynamic, central pool of lipids. An opening at this lipid rich region between YidC and the SecY lateral gate may provide an exit gateway for newly synthesized, correctly oriented, membrane protein helices to emerge from the HTL.
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