Direct interaction between two Escherichia coli transcription antitermination factors, NusB and ribosomal protein S10.
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.
Mason
S W
SW
Department of Molecular and Medical Genetics, University of Toronto, Canada.
Li
J
J
Greenblatt
J
J
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
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