In the lab, we are using a multidisciplinary approach to investigate proteins and protein complexes with essential functions during germ cell formation and early embryonic development. The research focusses on molecular mechanism such as piRNA-mediated transposon silencing and translation control of mRNAs, which are essential during early animal development.
In particular, we are currently focusing ours studies on LOTUS domain-containing proteins and on RNA helicases. To unravel the molecular mechanisms of how these proteins function, we employ a multidisciplinary approach combining RNA/protein biochemistry, X-ray crystallography, cell culture techniques as well as
Drosophila genetics.
Twitter @Jeske_Lab
Jeske, M. (2021). Molecular functions of germline proteins. EU Research. SPR21, 18.
Jeske, M. (2021). Molekulare Funktionen von Keimbahn-spezifischen Proteinen. BIOspektrum. 27, 101.
Kubíková, J., Reinig, R., Salgania, H.K., and Jeske, M. (2020). LOTUS-domain proteins - Developmental effectors from a molecular perspective. Biol. Chem. 402, 7–23.
Jeske, M., Müller, C.W., Ephrussi, A. (2017). The LOTUS domain is a conserved DEAD-box RNA helicase regulator essential for the recruitment of Vasa to the germ plasm and nuage. Genes Dev. 31(9), 939-952.
Jeske, M., Bordi, M., Glatt, S., Müller, S., Rybin, V., Müller, C.W., Ephrussi, A. (2015). The crystal structure of the Drosophila germline-inducer Oskar identifies two domains with distinct Vasa helicase- and RNA-binding activities. Cell Rep. 12(4), 587-98.
Jeske, M., Temme, C., Wahle, E. (2014). Assaying mRNA deadenylation in vitro. Methods Mol. Biol. 1125, 297–311.
Buschmann, J., Moritz, B., Jeske, M., Lilie, H., Schierhorn, A., Wahle, E. (2013). Identification of Drosophila and human 7-methyl GMP-specific nucleotidases. J. Biol. Chem. 288(4), 2441-2451.
Jeske, M., Moritz, B., Anders, A., Wahle, E. (2011). Smaug assembles an ATP-dependent stable complex repressing nanos mRNA translation at multiple levels. EMBO J. 30(1), 90-103.
Jeske, M., Wahle, E. (2008). Cell-free deadenylation assays with Drosophila embryo extracts. Meth. Enzymol. 448, 107-118.
Jeske, M., Meyer, S., Temme, C., Freudenreich, D., Wahle, E. (2006). Rapid ATP-dependent deadenylation of nanos mRNA in a cell-free system from Drosophila embryos. J. Biol. Chem. 281(35), 25124-25133.