Saskia Rödl - PhD Student

Tel.: +49 (0)631-205-2880
Email: s.roedl[at]rptu.de
roedl[at]rhrk.uni-kl.de
Room: 13-455

Project description:

Yeast can produce energy either by respiration or fermentation, depending on the carbon source availability. Changing the carbon source causes a variety of changes in the cells, including protein expression and degradation. So far, there is much known about cellular adaptations to respiratory growth conditions but not vice versa. In this context my study will focus on cellular modulations caused by changing growth conditions from respiration to fermentation. I’m particularly interested in glucose-induced protein degradation and its connection to the regulation of mitochondrial biogenesis.

Büsra Kizmaz - PhD Student

Tel.: +49 (0)631-205-2880
Email: b.kizmaz[at]rptu.de
bguengoe[at]rhrk.uni-kl.de
Room: 13-455

Project description:

Mitochondria are essential organelles of eukaryotes and play important roles in metabolism and signaling. Their function depends largely on a continuous flux of metabolites, nucleotides, and cofactors into and out of the organelle. Members of the mitochondrial carrier family facilitate the transport of a variety of metabolites through the inner membrane. These carrier proteins in turn need to be expressed and translocated to the inner mitochondrial membrane to fulfill their function. The aim of my study is to elucidate the cytosolic targeting of carrier proteins and their translocation through the outer mitochondrial membrane and a distinct translocase of the inner membrane, the TIM22 complex.

Anna-Lena Heußer - PhD Student

Tel.: +49 (0)631-205-2797
Email: annalena.ecker[at]rptu.de
ecker[at]rhrk.uni-kl.de
Room: 13-430

Project description:

Mitochondria are essential organelles of eukaryotic cells. As a relic of their a-proteobacterial origin, mitochondria still contain a small genome. In S. cerevisiae, the mitochondrial genome encodes for seven hydrophobic subunits of the respiratory chain and a ribosomal protein. However, in order to fulfill the multitude of mitochondrial functions, more than 900 mitoproteins are nuclear encoded, cytosolically translated and subsequently imported into mitochondria. The main question of my study is to find out why not all mitochondrial proteins have been transferred to the nuclear genome. Therefore, the aim of my project is to investigate if it is possible to cytosolically express hydrophobic mitochondrial encoded proteins, mainly Cox2, Cox3 and Atp6, and subsequently target and import them into mitochondria.

Svenja Lenhard - PhD Student

Tel.: +49 (0)631-205-2409
Email: s.lenhard[at]rptu.de
lenhard[at]rhrk.uni-kl.de
Room: 13-451

Project description:

Mitochondria consist of many hundreds of different proteins that are synthesized on cytosolic ribosomes. Mechanisms of protein translocation into these organelles have been intensively studied as they are essential for cellular function in eukaryotes. Precursor proteins can reach the inside of mitochondria either after their complete synthesis (post-translational) or simultaneous to their synthesis (co-translational). Although the import across the outer and inner mitochondrial membrane is well characterized, the processes occurring right before the translocation of a polypeptide remain unclear. Therefore, the aim of my work is to better understand how different precursors are sequestered to the mitochondrial surface and what determines post- or co-translational import.

Pavel Simakin - PhD Student

Tel.: +49 (0)631-205-2409
Email: p.simakin[at]rptu.de
simakin[at]rhrk.uni-kl.de
Room: 13-451

Project description:

Modular Cloning (MoClo) allows the combinatorial assembly of plasmids from standardized genetic parts. It is a very powerful strategy which enables highly flexible expression patterns without the need of repetitive cloning procedures. In this study, I enlarged the yeast toolkit and added sequence parts for the reliable intracellular targeting of proteins. The results appeared to be highly promising since as the MoClo approach allows it to optimize protein expression by finding the perfect combination of promoters, targeting sequences, epitope tags and vector backbones in simple, multiplexed approaches.

Annika Nutz - PhD Student

Tel.: +49 (0)631-205-2111
Email: anutz[at]rptu.de
Room: 13-432

Project description:

Carrier proteins, integral to the inner mitochondrial membrane, originate in the cytosol and are subsequently translocated to the mitochondria via the Tim22 carrier import pathway. Unlike preproteins which possess a cleavable, N-terminal targeting sequence, these mitochondrial carriers are characterized by at least one internal signal sequence located in either intermediate positions or adjacent to the C-terminus. The initial stages of carrier import, however, remain somewhat ambiguous. It is likely that a complex network of chaperones and targeting factors in the cytosol is required to ensure the accurate translocation of carrier precursors. The aim of my research is to delve deeper into the mechanisms underlying carrier biogenesis.

Lorenz Wagner - PhD Student

Tel. +49 (0)631-205-2797
Email: lowagner[at]rptu.de
Room: 13-430

Project description:

My project focuses on elucidating the intricacies of protein translocation into mitochondria, a critical process in eukaryotic cellular function. While the import across mitochondrial membranes is well-understood, the events leading up to protein translocation remain unclear. To address this gap, I will employ a proximity labeling approach to identify the interactome of Tom70 in the physiological context of yeast cells. I aim to utilize novel methods to overcome problems with APEX2-based proximity labeling in vivo. Thereby discovering yet unknown functional aspects, potential substrates, and interaction partners of Tom70.

Annika Egeler - PhD Student

Tel.: +49 (0)631-205-2797
Email: aegeler[at]rptu.de
Room: 13-430

Project description:

Most mitochondrial proteins pass the outer membrane via the Translocase of the Outer Membrane (TOM) complex and the inner membrane via the Translocase of the Inner Membrane(TIM23)complex. However, proteins destined for the inner membrane do not fully traverse TIM23; instead, they can be laterally inserted into the membrane through a process known as stop-transfer. Recent advances have identified Tim17, a hemi-channel forming protein, as the critical component for either membrane insertion or translocation into the matrix. However, the molecular details of how Tim17 sorts and inserts proteins into the membrane remain poorly understood. Thus, my aim is to elucidate the molecular mechanisms and factors involved in the sorting and insertion of translocation intermediates into the inner mitochondrial membrane.