title: Direct interaction between two Escherichia coli transcription antitermination factors, NusB and ribosomal protein S10.
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.
authors.affiliation: Department of Molecular and Medical Genetics, University of Toronto, Canada.
authors.forename: S W
authors.initials: SW
authors.lastname: Mason
authors.forename: J
authors.initials: J
authors.lastname: Li
authors.forename: J
authors.initials: J
authors.lastname: Greenblatt
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics*; D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D009154:Mutation; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012269:Ribosomal Proteins / Q000235:genetics*; D013728:Terminator Regions, Genetic; D014157:Transcription Factors; D014158:Transcription, Genetic
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C074952:NusB protein, E coli; D011993:Recombinant Fusion Proteins; D012269:Ribosomal Proteins; D014157:Transcription Factors; C029537:ribosomal protein S10