InstructThe latest webinar in the Instruct-ERIC Structure Meets Function series is hosted by Instruct-FR1. The webinar series offers an insight into the very cutting edge of structural biology research, utilising the latest techniques available through Instruct-ERIC facilities and centres.
This month will two speakers who have accessed the IGBMC facility at Instruct-FR1. Find out more about the technologies available at the centre, and the expert contacts who can help with your research project.
The webinar will take place 11:00-12:00 CET, on 23 January. Register here.
Take a look at the other webinars in the series here.
Speaker 1: Katia Zanier - Université de Strasbourg
Title: Mechanism of IKK kinase-substrate docking in NF-kB signaling
Abstract: The inhibitor of kB kinase (IKK) complex is the master regulator of NF-kB signaling and plays a fundamental role in inflammatory processes and in the innate immune response. All IKK complexes contain hetero- or homodimers of the catalytic IKKβ and/or IKKα subunits. We have identified a novel small linear motif, which mediates docking of key substrates of the canonical (IkBα, IkBβ) and alternative (p100) NF-kB pathways to catalytic IKK dimers. Results from integrated structural analyses indicate that the motif binds to a groove at the IKK dimer interface. This work unveils a function for IKKα∫β dimerization in substrate recruitment and therefore activation of NF-kB transcription.
Speaker 2: Konstantin Brodolin - Université de Montpellier
Title: Regulation of transcription via RNA polymerase oligomerization
Abstract: Self-assembly of macromolecules into higher-order symmetric structures is fundamental for the regulation of biological processes. Higher-order symmetric structure self-assembly by the gene expression machinery, such as bacterial DNA-dependent RNA polymerase (RNAP), has never been reported before. We found that the stress-response transcription factor, σB, from the human pathogen, Mycobacterium tuberculosis, induces RNAP oligomerization into a supramolecular complex composed of eight RNAP units. Cryo-electron microscopy revealed a pseudo-symmetric structure of the RNAP octamer in which RNAP protomers are captured in an auto-inhibited state. Our results demonstrate how basal transcription factors can regulate gene expression by modulating the RNAP holoenzyme assembly and hibernation.
