Intrinsically disordered proteins (IDPs) are most famous for their involvement in misfolding neurodegenerative ageing diseases like Alzheimer, Parkinson and Huntington. Almost paradoxically, IDPs are key to many important and precise cellular mechanisms, such as nuclear transport, chromatin packaging, epigenetic regulation and the stress response. Our current understanding is that the ability to encode multiple functions and complexity into these dynamic polymer-like proteins apparently outweighs the seeming disadvantages and risks of misfolding, the chances of which increase with molecular and cellular age. The dynamic nature of IDPs makes their experimental characterisation very difficult, as classical technologies in structural biology like X-ray crystallography and electron microscopy (EM) are limited to largely static systems. Consequently, the disordered part of the proteome remains largely inaccessible to us, constituting what we refer to as the “Dark Proteome”.
Our group uses a multidisciplinary approach centered around superresolved fluorescence technologies, chemical and synthetic biology, microscope and microfluidic engineering to study functional IDPs in eukaryotes, such as in nuclear transport and gene regulation. We aim to understand how function can be encoded into the protein sequence of a seemingly floppy protein and how the cell balances the intrinsic risk of these proteins becoming dysfunctional and ageing to toxic states like the amyloid phenotype.
- Since 2018: Adjunct Director, Institute of Molecular Biology (IMB) & Professor of Synthetic Biophysics, Johannes Gutenberg University (JGU), Mainz
- 2009 - 2020: Group Leader, EMBL, Heidelberg
- 2005 - 2008: Research Associate (Postdoc), The Scripps Research Institute, La Jolla
- 2005: PhD MPI for Biophysical Chemistry and University of Göttingen
- 2001: Diploma in Chemistry, Technical University of Berlin
- 2001: Master of Science, University of Oklahoma
Selected publications by Edward Lemke
Reinkemeier CD and Lemke EA (2021) Dual film-like organelles enable spatial separation of orthogonal eukaryotic translation. Cell, 184:1–18 Link
Reinkemeier CD, Girona GE and Lemke EA (2019) Designer membraneless organelles enable codon reassignment of selected mRNAs in eukaryotes. Science, 363:eaaw2644 Link
Tan PS, Aramburu IV, Mercadante D, Tyagi S, Chowdhury A, Spitz D, Shammas SL, Gräter F and Lemke EA (2018) Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors. Cell Rep, 22:3660–3671 Link
Koehler C, Sauter PF, Wawryszyn M, Girona GE, Gupta K, Landry JJM, Fritz MH-Y, Radic K, Hoffmann J-E, Chen ZA, Zou J, Tan PS, Galik B, Junttila S, Stolt-Bergner P, Pruneri G, Gyenesei A, Schultz C, Biskup MB, Besir H, Benes V, Rappsilber J, Jechlinger M, Korbel JO, Berger I, Braese S and Lemke EA (2016) Genetic code expansion for multiprotein complex engineering. Nat Methods, 13:997–1000 Link
Milles S, Mercadante D, Aramburu IV, Jensen MR, Banterle N, Koehler C, Tyagi S, Clarke J, Shammas SL, Blackledge M#, Gräter F# and Lemke EA# (2015) Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors.Cell, 163:734–745 (# indicates joint correspondence) Link
Lemke lab website