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- W2023396205 abstract "Protein S10 is a component of the 30S ribosomal subunit and participates together with NusB protein in processive transcription antitermination. The molecular mechanisms by which S10 can act as a translation or a transcription factor are not understood. We used complementation assays and recombineering to delineate regions of S10 dispensable for antitermination, and determined the crystal structure of a transcriptionally active NusB-S10 complex. In this complex, S10 adopts the same fold as in the 30S subunit and is blocked from simultaneous association with the ribosome. Mass spectrometric mapping of UV-induced crosslinks revealed that the NusB-S10 complex presents an intermolecular, composite, and contiguous binding surface for RNAs containing BoxA antitermination signals. Furthermore, S10 overproduction complemented a nusB null phenotype. These data demonstrate that S10 and NusB together form a BoxA-binding module, that NusB facilitates entry of S10 into the transcription machinery, and that S10 represents a central hub in processive antitermination." @default.
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- W2023396205 date "2008-12-01" @default.
- W2023396205 modified "2023-10-16" @default.
- W2023396205 title "Structural and Functional Analysis of the E. coli NusB-S10 Transcription Antitermination Complex" @default.
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- W2023396205 doi "https://doi.org/10.1016/j.molcel.2008.10.028" @default.
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