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首页> 外文期刊>Journal of Molecular Biology >Efficient transcriptional antitermination from the Escherichia coli cytoplasmic membrane
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Efficient transcriptional antitermination from the Escherichia coli cytoplasmic membrane

机译：大肠杆菌细胞质膜的高效转录抗终止

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The BglG protein is a transcriptional antiterminator acting within the beta -glucoside operon of Escherichia coli by binding to a specific sequence motif in the growing mRNA. Binding of BglG prevents formation of the terminator stem-loop structure, thereby causing the RNA polymerase to continue transcription. Activity of BglG is modulated in a complex way by antagonistically acting phosphorylations in response to the availability of beta -glucosidic substrates and to the catabolic state of the cell. The enzymes responsible for these phosphorylations are members of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) that represents a central carbohydrate uptake and signal transduction system. As these enzymes are believed to all form higher-order complexes associated with the cytoplasmic membrane, we tested whether or not BglG would remain active when artificially anchored to its presumptive site of regulation, the inner membrane. We show that the membrane-anchored protein indeed efficiently catalyzes transcriptional antitermination. Moreover, the membrane-attached BglG remains regulated by the PTS. Thus, a membrane-bound regulatory RNA binding protein can potentially interact fast enough with its target within the nascent transcript and cause the transcriptional machinery to proceed, before transcriptional termination would occur. Consequently, there is no principal necessity for an RNA-binding transcriptional regulator like BglG to leave the inner membrane, a potential regulatory site, and migrate to the site of transcription, the nucleoid. (C) 2001 Academic Press. [References: 65]
机译：BglG蛋白是一种转录抗终止剂，通过与生长的mRNA中的特定序列基序结合，在大肠杆菌的β-葡萄糖苷操纵子内起作用。 BglG的结合阻止了终止子茎环结构的形成，从而导致RNA聚合酶继续转录。通过响应于β-葡萄糖苷底物的可用性和细胞的分解代谢状态，通过拮抗作用的磷酸化以复杂的方式调节BglG的活性。负责这些磷酸化的酶是磷酸烯醇丙酮酸：碳水化合物磷酸转移酶系统（PTS）的成员，代表中央碳水化合物的摄取和信号转导系统。由于相信这些酶均会形成与细胞质膜相关的高级复合物，因此我们测试了BglG在人工锚定至其推测的调节位点即内膜时是否仍将保持活性。我们表明，膜锚定的蛋白质确实有效地催化转录抗终止。此外，膜连接的BglG仍受PTS调控。因此，在发生转录终止之前，膜结合的调节性RNA结合蛋白可能会与其新生转录物中的靶标相互作用足够快，并导致转录机制继续进行。因此，不需要像BglG这样的RNA结合转录调节子离开内膜，即潜在的调节位点，并迁移到转录位点，即类核苷酸。 （C）2001学术出版社。 [参考：65]

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