Abstract
The transcriptional antitermination protein N of bacteriophage lambda binds the boxB component of the RNA enhancer nut (boxA + boxB) and the E. coli elongation factor NusA. Efficient antitermination by N requires an RNA-binding domain (amino acids 1-22) and two activating regions for antitermination: a newly identified NusA-binding region (amino acids 34-47) that suppresses NusA's enhancement of termination, and a carboxy-terminal region (amino acids 73-107) that interacts directly with RNA polymerase. Heteronuclear magnetic resonance experiments demonstrate that N is a disordered protein. Interaction with boxB RNA induces only the RNA-binding domain of N to adopt a folded conformation, while the activating regions of the protein remain disordered in the absence of their target proteins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism
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Bacteriophage lambda / chemistry*
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Bacteriophage lambda / enzymology
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Bacteriophage lambda / genetics*
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Binding Sites / physiology
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DNA-Directed RNA Polymerases / metabolism
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Enhancer Elements, Genetic / physiology
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Escherichia coli Proteins
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Gene Expression Regulation, Viral*
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Ligands
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Magnetic Resonance Spectroscopy
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Molecular Sequence Data
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Peptide Elongation Factors*
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Peptide Fragments / metabolism
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Protein Structure, Tertiary
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RNA, Viral / chemistry
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RNA, Viral / genetics
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RNA, Viral / metabolism
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Regulatory Sequences, Nucleic Acid
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Transcription Factors / chemistry
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Transcription Factors / metabolism
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Transcriptional Elongation Factors
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Viral Regulatory and Accessory Proteins / chemistry*
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Viral Regulatory and Accessory Proteins / genetics
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Viral Regulatory and Accessory Proteins / metabolism*
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Ligands
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N protein, Bacteriophage lambda
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Peptide Elongation Factors
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Peptide Fragments
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RNA, Viral
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Transcription Factors
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Transcriptional Elongation Factors
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Viral Regulatory and Accessory Proteins
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nusA protein, E coli
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DNA-Directed RNA Polymerases