Abstract
The Escherichia coli proteins NusB and ribosomal protein S10 are important for transcription antitermination by the bacteriophage lambda N protein. We have used sucrose gradient co-sedimentation and affinity chromatography with immobilized ribosomal protein S10, a glutathione S-transferase-S10 fusion protein, and NusB to show that NusB binds directly and very selectively to S10. The interaction is non-ionic and has an estimated Kd value of 10(-7) M. We hypothesize that NusB binds to N-modified transcription complexes primarily by interacting with S10.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / genetics*
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Chromatography, Affinity
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Escherichia coli / genetics*
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Escherichia coli Proteins*
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Gene Expression Regulation, Bacterial*
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Mutation
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Protein Binding
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Recombinant Fusion Proteins / metabolism
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Ribosomal Proteins / genetics*
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Terminator Regions, Genetic*
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Transcription Factors
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Transcription, Genetic*
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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NusB protein, E coli
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Recombinant Fusion Proteins
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Ribosomal Proteins
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Transcription Factors
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ribosomal protein S10