CSL proteins [named after the homologs CBF1 (RBP-Jκ in mice), Suppressor of Hairless and LAG-1] are conserved transcription factors found in animals and fungi. In the fission yeast Schizosaccharomyces pombe, they regulate various cellular processes, including cell cycle progression, lipid metabolism and cell adhesion. CSL proteins bind to DNA through their N-terminal Rel-like domain and central β-trefoil domain. Here, we investigated the importance of DNA binding for CSL protein functions in fission yeast. We created CSL protein mutants with disrupted DNA binding and found that the vast majority of CSL protein functions depend on intact DNA binding. Specifically, DNA binding is crucial for the regulation of cell adhesion, lipid metabolism, cell cycle progression, long non-coding RNA expression and genome integrity maintenance. Interestingly, perturbed lipid metabolism leads to chromatin structure changes, potentially linking lipid metabolism to the diverse phenotypes associated with CSL protein functions. Our study highlights the critical role of DNA binding for CSL protein functions in fission yeast.

Center for Inflammatory Skin Diseases Department of Dermatology and Allergy University Hospital Schleswig Holstein Campus Kiel Rosalind Franklin Straße 9 24105 Kiel Germany

Department of Cell Biology Faculty of Science Charles University Viničná 7 128 00 Prague 2 Czechia

Department of Cellular and Molecular Biology Centro de Investigaciones Biológicas Margarita Salas Consejo Superior de Investigaciones Científicas Ramiro de Maeztu 9 28040 Madrid Spain

Institute of Healthy Ageing and Department of Genetics Evolution and Environment University College London Gower Street London WC1E 6BT UK

Laboratory of Genomics and Bioinformatics Institute of Molecular Genetics of the Czech Academy of Sciences Vídeňská 1083 142 20 Prague 4 Czechia

Citace poskytuje Crossref.org

Cbf11 and Mga2 function together to activate transcription of lipid metabolism genes and promote mitotic fidelity in fission yeast