Ronald S. Johnson, PhD
The Brody School of Medicine at East Carolina University
Greenville, NC 27834
- B.A., Northwestern Univ., 1973
- Ph.D., Northwestern Univ., 1978
Mechanism of action of Escherichia coli RNA polymerase
- regulation of gene expression
- reaction mechanisms
- physical biochemistry
The regulation of gene expression at the level of transcription is a central problem in biochemistry. The key element in this process is RNA polymerase. Greater insight into this process can be obtained by investigating the structural, thermodynamic and kinetic parameters associated with the various stages of transcription; i.e. promoter site binding, initiation, promoter clearance, elongation and termination. Our major focus is on an investigation of the mechanisms of initiation and elongation/translocation as well as on an investigation of the molecular mechanism for the fidelity of transcription. We are using a combination of fluorescence spectroscopy, stopped-flow and quench-flow kinetics, enzymatic assays, protein chemistry and molecular biology in our studies on the molecular mechanism of transcription as catalyzed by E. coli RNA polymerase.
Johnson, R. S., Strausbauch, M. & McCloud, C. (2022). An NTP-driven mechanism for the nucleotide addition cycle of Escherichia coli RNA polymerase during transcription. PLoS One, 17(10):e0273746. https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0273746.
Johnson, R. S., Strausbauch, M. & Register, J. K. (2011). Rapid Pyrophosphate Release from Transcriptional Elongation Complexes Appears to be Coupled to a Nucleotide-Induced Conformational Change in E. coli Core Polymerase. J. Mol. Biol. 412, 849-861. https://doi.org/10.1016/j.jmb.2011.05.023
Johnson, R.S., Strausbauch, M., Cooper, R. and Register, J.K. (2008). Rapid Kinetic Analysis of Transcription Elongation by Esherichia coli RNA Polymerase. J. Mol. Biol. 381, 1106-1113.
Johnson, R. S. and Chester, R. E. (2002). UTP Allosterically Regulates Transcription by Escherichia coli RNA Polymerase from the Bacteriophage T7 A1 Promoter. J. Mol. Biol. 318, 305-320 (PDF).
Johnson, R. S. and Chester, R. E. (1998). Stopped-flow kinetic analysis of the interaction of Escherichia coli RNA polymerase with the bacteriophage T7 A1 promoter. J. Mol. Biol. 283, 353-370.
Johnson, R. S. (1991). Nonspecific interaction of Escherichia coli pyrenyl RNA polymerase holoenzyme with synthetic polynucleotides as monitored by fluorescence spectroscopy. Biochemistry 30, 198-206.
Johnson, R. S., Bowers, M. and Eaton, Q. (1991). Preparation and characterization of N-(1-Pyrenyl)iodoacetamide-labeled Escherichia coli RNA polymerase. Biochemistry 30, 189-198.