Article
Mutational analysis of Escherichia coli GreA protein reveals new functional activity independent of antipause and lethal when overexpressed.
Scientific reports - 30 Sept 2020
Fernández-Coll Llorenç, Potrykus Katarzyna, Cashel Michael, Balsalobre Carlos
Abstract excerpt
There is a growing appreciation for the diverse regulatory consequences of the family of proteins that bind to the secondary channel of E. coli RNA polymerase (RNAP), such as GreA, GreB or DksA. Similar binding sites could suggest a competition between them. GreA is characterised to rescue stalled RNAP complexes due to its antipause activity, but also it is involved in transcription fidelity and proofreading....
Topics
- Binding, Competitive
- DNA Mutational Analysis
- DNA-Directed RNA Polymerases
- Escherichia coli
- Escherichia coli Proteins
- Gene Deletion
- Gene Expression Regulation, Bacterial
- Genes, Bacterial
- Genes, Lethal
- Genetic Variation
- Models, Molecular
- Mutagenesis