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首页> 外文期刊>Journal of bacteriology >Archaeal Binding Protein-Dependent ABC Transporter: Molecular and Biochemical Analysis of the Trehalose/Maltose Transport System of the Hyperthermophilic Archaeon Thermococcus litoralis
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Archaeal Binding Protein-Dependent ABC Transporter: Molecular and Biochemical Analysis of the Trehalose/Maltose Transport System of the Hyperthermophilic Archaeon Thermococcus litoralis

机译：古细菌结合蛋白依赖的ABC转运蛋白：超嗜热古细菌热球菌海藻糖/麦芽糖转运系统的分子和生化分析。

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摘要

We report the cloning and sequencing of a gene cluster encoding a maltose/trehalose transport system of the hyperthermophilic archaeonThermococcus litoralis that is homologous to themalEFG cluster encoding the Escherichia colimaltose transport system. The deduced amino acid sequence of themalE product, the trehalose/maltose-binding protein (TMBP), shows at its N terminus a signal sequence typical for bacterial secreted proteins containing a glyceride lipid modification at the N-terminal cysteine. The T. litoralis malE gene was expressed in E. coli under control of an inducible promoter with and without its natural signal sequence. In addition, in one construct the endogenous signal sequence was replaced by the E. coli MalE signal sequence. The secreted, soluble recombinant protein was analyzed for its binding activity towards trehalose and maltose. The protein bound both sugars at 85°C with aKd of 0.16 μM. Antibodies raised against the recombinant soluble TMBP recognized the detergent-soluble TMBP isolated from T. litoralis membranes as well as the products from all other DNA constructs expressed in E. coli. Transmembrane segments 1 and 2 as well as the N-terminal portion of the large periplasmic loop of the E. coli MalF protein are missing in the T. litoralis MalF. MalG is homologous throughout the entire sequence, including the six transmembrane segments. The conserved EAA loop is present in both proteins. The strong homology found between the components of this archaeal transport system and the bacterial systems is evidence for the evolutionary conservation of the binding protein-dependent ABC transport systems in these two phylogenetic branches.
机译：我们报告了编码与嗜热古细菌 litoralis litoralis 的麦芽糖/海藻糖转运系统基因簇的克隆和测序，该基因簇与编码埃希氏菌的 malEFG 簇同源大肠杆菌麦芽糖运输系统。推导的 malE 产品的氨基酸序列，海藻糖/麦芽糖结合蛋白（TMBP），在其N端显示典型的细菌分泌蛋白的信号序列，该蛋白在N-端含有甘油脂修饰末端半胱氨酸。 T。 litoralis malE 基因在 E中表达。诱导型启动子的控制下，带有或不带有其天然信号序列的大肠杆菌。另外，在一种构建体中，内源信号序列被 E替代。大肠杆菌MalE信号序列。分析了分泌的可溶性重组蛋白对海藻糖和麦芽糖的结合活性。该蛋白在85°C以0.16μM的 K d 结合两种糖。针对重组可溶性TMBP产生的抗体识别出分离自 T的去污剂可溶性TMBP。 litoralis 膜以及在 E中表达的所有其他DNA结构的产物。大肠杆菌。跨膜片段1和2以及 E大周质环的N末端部分。 T中缺少大肠杆菌 MalF蛋白。锦葵 MalF。 MalG在整个序列（包括六个跨膜片段）中都是同源的。两种蛋白质中均存在保守的EA​​A环。在该古细菌运输系统的各组成部分和细菌系统之间发现的强同源性，为这两个系统发生分支中结合蛋白依赖性ABC运输系统的进化保守性提供了证据。

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