This fixed-term position is initially available for 9 months, with the possibility for extension. The project aim is to integrate and analyse numerous existing in-house datasets comprising RNA-seq, single cell transcriptomics and genomic resources, as well as to set up a user-friendly interface for the labs’ bioinformatics resources and workflows. The position is available for early-career scientists holding a PhD-degree.

We are seeking a postdoc for a project entitled: Shedding light on corals: How DNA damage repair, cryptochromes and the circadian clock shape the response of Anthozoa to sunlight.

We are seeking a Research Associate working on projects focusing on the evolutionary aspects of the cnidarian-dinoflagellate symbiosis using Aiptasia anemones as an experimental model and comparative approaches based on related system and/or field-based studies.

The successful candidate will use genetic code expansion, structural and biophysical techniques, and cell-based assays to unravel how HSP90 is regulated by acetylation. (S)he will use targeted mass spectrometry to identify HSP90 acetylation, express and purify HSP90 variants, analyze structural and functional consequences of HSP90 acetylation, and characterize in detail interactions between HSP90 and HDACs. The candidate will be enrolled in a PhD program at the Charles University in Prague.

The successful candidate will use heterologous expression to prepare different TTLL11s variants to reconstitute the TTLL11/tubulin system in vitro and to provide structural insights into tubulin recognition by TTLL11. TIRF microscopy will be used to analyze the influence of polyglutamylation on microtubule characteristics and their interactions with microtubules associated proteins. Generation of CRISPR/Cas9 TTLL11-targeted knock-in cell lines will be exploited to shed a light onto phase separation of TTLL11 as well as to identify novel TTLL11 physiological substrates via proximity-based labeling. The candidate will be enrolled in a PhD program at the Charles University in Prague.

You will co-lead a project aimed at structure-function and physiological studies of zinc-dependent histone deacetylases (HDACs). You will use purified target HDACs from various organisms and profile their substrate specificity. Mutagenesis, biophysical approaches, structural biology techniques, and genetic code expansion technology will be used to understand recognition of substrates at the protein level. The acquired knowledge will be used to develop of isoform- as well as organism-specific HDAC inhibitors. Metabolomics and lipidomics will complement in vitro findings in our search for unknown physiological substrates and roles of HDACs. You will contribute to supervision of junior colleagues, manuscript writing, and present your results at meetings.

You will co-lead a project aimed at structure-function studies of anterograde transport mediated by conventional kinesins and their interactions with cargo molecules. You will use a bottom-up approach to reconstitute a kinesin/cargo transport system using purified protein components to and analyze their structural and functional properties. The TIRF will be used to visualize the complexes and elucidate their functional properties up to the single molecule level and neuronal cell-based assays to translate and validate data in physiological environment of the axonal transport. You will contribute to supervision of junior colleagues, manuscript writing, and present your results at meetings.

We are currently looking for enthusiastic M.A. and Ph.D. students!

We are looking for a laboratory manager/technician for maintaining the smooth work of the group as well as for performing experiments in our protein cage engineering projects. The work tasks include maintenance of research materials and instruments in the laboratory, preparation of general lab stocks, teaching experimental techniques and safety rules to students, as well as performing experiments under the supervision of the project leader. The ideal candidate should have at least 2-year work experience in a wet laboratory conducting molecular cloning and recombinant protein production.