Dohmen lab - Institute for Genetics
Regulation of Substrate Targeting Modes of SUMO Protease Ulp2
Conjugation to small ubiquitin-related modifier (SUMO) is an essential posttranslational protein modification that controls localization and functions of proteins in eukaryotic cells. SUMOylation is reversible by the action of deSUMOylating enzymes, Ulp1 and Ulp2 in yeast. We have studied the structure and function of Ulp2 and found that it can act on distinct types of SUMOylated proteins. In this project, we will investigate how localization and substrate selection modes of the Ulp2 enzyme are regulated posttranslationally.
First Cohort Project: Polysumoylation-Mediated Relocalization of Proteins to the Nucleus
Protein modification with the small ubiquitin-related modifier (SUMO) is an essential reversible regulatory mechanism in eukaryotic cells known to cross-talk to other PTMs such as ubiquitylation, phosphorylation, and acetylation. Fluorescent reporter proteins fused to SUMO chains are strongly enriched in the cell nucleus. The goal of this project is to elucidate the mechanism of polysumoylation-mediated nuclear translocation and to investigate its reversibility.
Maximilian Haka
PhD Students since October 2023
EMail: mhaka[at]smail.uni-koeln.de
"I was always fascinated by science and nature, so I set out to study Biological Sciences at the University of Cologne, were I obtained my Bachelor`s and Master`s Degree. I quickly learned that my passion was molecular biology and genetics, working with proteins and unraveling their characteristics. My doctoral research in the Dohmen lab revolves around the posttranslational modifier SUMO and its regulation, more specifically, I study the deSUMOylating enzyme Ulp2 which removes SUMO from substrates in a specific manner."
Friederike Profe
PhD student since April 2020
EMail: fprofe1[at]uni-koeln.de
"I am Friederike and currently doing my PhD in the group of Prof. Dohmen. Before, I studied Biochemistry in Jena and Cologne. My main interest is the regulation of cellular mechanisms, many of which are controlled through intricate cascades and rely on precise modification of proteins. Those control mechanisms open up a very fascinating world, of which I love being able to explore a small fraction during my PhD."
Lennard-Maximilian Döring
Graduated in January 2023
EMail: doeringl[at]smail.uni-koeln.de
"I studied biology at the university of Cologne, with a focus on genetics and microbiology. Fortunately, I had the opportunity to pursue my master's project in the Dohmen Lab, in which we aimed to understand the dynamic modification of proteins with the Small Ubiquitin-like modifier (SUMO)."
Publications:
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Hypusinated eIF5A Promotes Ribosomal Frameshifting during Decoding of ODC Antizyme mRNA in Saccharomyces cerevisiae. Halwas K, Döring LM, Oehlert FV, Dohmen RJ. Int J Mol Sci. 2022 Oct 26;23(21):12972. doi: 10.3390/ijms232112972. PMID: 36361762
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Methods to study SUMO dynamics in yeast. Pabst S, Döring LM, Petreska N, Dohmen RJ. Methods Enzymol. 2019;618:187-210. doi: 10.1016/bs.mie.2018.12.026. Epub 2019 Feb 11. PMID: 30850052
Selected Publications Dohmen lab
- Pabst, S., L.M. Döring, N. Petreska, R.J. Dohmen (2019), Methods to study SUMO dynamics in yeast. Methods Enzymol. 618: p. 187-210.
- Eckhoff, J. and R.J. Dohmen (2015), In Vitro Studies Reveal a Sequential Mode of Chain Processing by the Yeast SUMO (Small Ubiquitin-related Modifier)-specific Protease Ulp2. J Biol Chem. 290(19): p. 12268-81.
- Sriramachandran, A.M., and R.J. Dohmen (2014), SUMO-targeted ubiquitin ligases. Biochim Biophys Acta.1843(1): p. 75-85.