6th Structural Biology Club of the Czech Society for Structural Biology on 24 November 2021

  • 24 November 2021

6th Structural Biology Club of the Czech Society for Structural Biology will be  online on 24 November 2021 at 13:00 with the following scientific talk kindly delivered by our guests:

Tau regulates access to microtubules

Presented by Zdeněk Lánský from the Institute of Biotechnology, Czech Academy of Sciences, Vestec

Tau is an intrinsically disordered microtubule-binding protein involved in a number of neurodegenerative diseases. Malfunction of tau and its detachment from axonal microtubules are correlated with axonal degeneration. However, mechanistic understanding of this process is still missing. We recently showed that tau molecules cooperatively form cohesive, selectively permeable, envelopes on the microtubule surface. Importantly, these tau envelopes can protect microtubules from microtubule-degrading enzymes. I will discuss the mechanism of the tau envelope formation and the roles of envelope in regulating the access to the microtubule surface.

 The role of IDP regions in nucleosome recognition

Presented by Václav Veverka from the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences and the Department of Cell biology, Faculty of Science, Charles University, Praha

Numerous aspects of nuclear organization are mediated by interactions involving structured as well as unstructured protein elements and DNA. The roles of intrinsically disordered protein regions are exemplified by the large number of unstructured protein regions that play essential roles within the nucleus, ranging from the C-terminal domain of RNA polymerase 2 to amphipathic repeats that drive liquid-liquid phase separation. Unlike the structured parts of proteins, the conformational plasticity of intrinsically disordered protein regions makes it almost impossible to capture them using cryo-electron microscopy and X-ray crystallography.  We combine cryo-electron microscopy and NMR spectroscopy to uncover the molecular mechanism of multivalent interactions between a chromatin reader protein LEDGF and H3K36-modified nucleosomes. Our data suggest a role for the intrinsically disordered LEDGF region in restraining the effective space for assembly of LEDGF-mediated transcriptional complexes.

Please, join us on this Zoom link (join 5-10 minutes before the beginning)

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Meeting ID: 934 8283 6889
Passcode: 983648

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