Richard Ebright
Rutgers University-New Brunswick, NJ·Biochemistry
Every gene that gets read into RNA must eventually stop being read. That stopping step, called transcription termination, decides where a gene ends and is one of the main ways cells control how much of each protein they make.
- Fields
Biochemistry
Microbiology & Immunology
Biophysics
- Topics
transcription termination
antitermination
RNA polymerase
- Grants
- 1 known grant, through Jun 2027
What they work on
- Determine structures of intact, functional factor-dependent pre-termination complexes from E. coli and the archaeon Thermococcus kodakarensis by cryo-electron microscopy, defining how the ATP-driven RNA motor Rho and the RNA-cutting enzyme aCPSF1 engage RNA polymerase.
- Define how intrinsic termination works, in which the new RNA folds into a hairpin followed by a run of U bases, by solving structures of complete bacterial pre-termination complexes and capturing intermediates between the pre- and post-termination states.
- Test competing mechanisms of release, that RNA polymerase is pushed forward, that RNA is pulled out, or that the enzyme changes shape, using single-molecule picometer-resolution nanopore tweezers to follow individual enzymes step by step along DNA.
- Define the structural basis of Q-dependent antitermination, in which a bacteriophage protein lets RNA polymerase read through stop signals, mapping the protein-DNA, protein-RNA, and protein-protein contacts involved.
More about the research
In bacteria and in archaea (single-celled organisms that resemble bacteria but are evolutionarily closer to us), the first steps of transcription are well mapped, but the final step is not. Work in this lab aims to fill that gap by capturing the molecular machines that halt transcription in the act.
Why it matters
Transcription is the most heavily regulated step in gene expression and is already the target of two classes of antibacterial drugs, so a mechanistic account of how bacteria stop transcription maps out territory where new antibacterial strategies could be sought. Because archaeal RNA polymerase closely resembles the human enzyme, the findings may also inform how transcription ends in our own cells.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Jia Fei
Rutgers University-New Brunswick, NJ·Biochemistry
Characterize how NDF loosens nucleosomes, the protein spools that package DNA, and helps RNA Polymerase II move through them, using ultra-high-resolution optical tweezers and cryo-electron microscopy.
Jie Xiao
Johns Hopkins University, MD·Biophysics
Measure how DNA supercoiling changes transcription speed and coupling between neighboring RNA polymerase molecules, using single-molecule imaging of purified RNA polymerase and DNA constructs.
Ruslan Afasizhev
Boston University, MA·Biochemistry
Define how complexes built around KRET1, an enzyme that adds U-tails to RNA, couple tailing with RNA degradation in the T. brucei mitochondrion, using proteomics, imaging, and cryo-EM.
The school
Rutgers University-New Brunswick: 57 labs on PI Pages, $837M a year on research, 713 research doctorates a year.
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