RNA polymerase, RNAP, is an enzyme complex responsible for synthesizing RNA molecules. RNAP copies RNA based on a DNA template during the process of transcription, a fundamental operation conserved from bacteria to humans.
Identifying specific interactions between RNAP and other proteins can lead to the discovery of new therapeutic targets for antibiotic development that are more effective and less prone to bacterial resistance. Additionally, understanding the mechanisms of resistance, which can arise from mutations altering interactions between RNA polymerase and other proteins, allows us to better address the problem of antibiotic resistance and develop new strategies to combat it [1, 2]. Finally, elucidating the role of RNAP and its protein complexes contributes to comprehensive understanding of bacterial biology.
Here, we discovered that a protein involved in protein translation that binds to RNAP, potentially linking the two processes in a not yet identified manner. Currently, we are characterizing the interactions between this protein and RNAP by biophysical and structural biology methods (cryo-EM, small-angle X-ray scattering, homologous modelling, etc.). In parallel, this interaction is being probed functionally by biochemical approaches.
This work was supported by CSF (23-06295S), AS CR (86652036), MEYS (LM2023042), ERDF (CZ.02.1.01/0.0/0.0/18_046/0015974), and by support of Biocev CMS core facilities Biophysical Methods, Structural Mass Spectrometry, Crystallization of Proteins and Nucleic Acids, Diffraction Techniques and of CEITEC, Masaryk University Cryo-electron microscopy and tomography core facility (CEMCOF), all of CIISB, part of Instruct-ERIC.