NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif

Article Abstract:

The structure of the bacteriophage lambda N peptide/boxB RNA complex was investigated using heteronuclear magnetic resonance spectroscopy. Nuclear magnetic resonance spectroscopy was also employed to determine the structures of the complexes formed by the arginine-rich motifs of the immunodeficiency virus Tat and HIV-1 Rev proteins with their RNA ligands. Results show that the GAAGA boxB loop forms a GNRA fold which is a requirement in N binding. The structure of the complex suggests new modes of RNA folding and RNA-protein recognition.

Physiological aspects, Peptides, RNA, Protein folding, Arginine

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Recognition of boxA antiterminator RNA by the E. coli antitermination factors NusB and ribosomal protein S10

Article Abstract:

The boxA sequences of the Escherichia coli ribosomal RNA (rrn) operon were investigated with respect to transcription antitermination in bacteriphage lambda. Polyacrylamide gel mobility shift experiments on RNA containing the boxA sequence were carried out with purified transcription factors NusA, NusB and NusG, and the ribosomal protein S10. The findings demonstrate that NusB and S10 interact specifically with the rrn boxA RNA. This interaction is required for transcription antitermination in the rrn operons.

Ribosomal proteins

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Function of E. coli RNA polymerase sigma factor sigma70 in promoter-proximal pausing

Article Abstract:

The sigma factor sigma70 of Escherichia coli RNA polymerase is more widely known for initiating RNA synthesis. However, its other roles includes inducing a transcription pause at an early stage of elongation, simultaneously allowing the phage delta gene Q transcription antiterminator to act. Experiments indicate that the factor is necessary for pausing and is present in the paused transcription complex.

RNA polymerases

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