Graduate Students Mini Symposium V 2021
- Datum: 06.09.2021
- Uhrzeit: 16:00
- Ort: Online
- Raum: -
- Gastgeber: IMPRS
- Kontakt: firstname.lastname@example.org
16:00 Florian Lindner (RG Diepold)
LITESEC-T3SS - Light-controlled protein delivery into eukaryotic cells with high spatial and temporal resolution
The type III secretion system (T3SS) is a needle-like structure that is used by many pathogenic gram-negative bacteria to translocate effector proteins into eukaryotic host cells. Recent studies have shown that the cytosolic complex of the T3SS acts as a highly dynamic interface, and that this dynamic behavior is linked to protein secretion. The combination of optogenetic interaction switches with a dynamic essential cytosolic component of the T3SS enables control of the T3SS function with light. With that, we developed a spatiotemporal resolved light-controllable protein delivery tool into eukaryotic host cells and presented the great potential of optogenetic applications in bacteria.
16:30 Ying Liu (RG Thanbichler)
Comprehensive analysis of bactofilin in Caulobacter crescentus
Bactofilin is a new class of bacterial cytoskeleton. Similar to other cytoskeletons, it is involved in the temporal and spatial organization of cellular machineries. In C. crescentus, bactofilin is implicated in the stalk biogenesis via the peptidoglycan remodeling enzyme PbpC. Structural studies have shown that the right-handed β-helical monomer of bactofilin can assemble into non-polar protofilaments. Despite our knowledge of its structure, many aspects about bactofilin remain enigmatic, such as the lateral interaction between protofilaments, the membrane association, and the interaction between bactofilin and its partner. In this project, various methods are employed to comprehensively analyze bactofilin in C. crescentus.
17:00 Ruth Breuer (RG Randau)
RNA-seq and biochemical analyses of (SRP) RNA processing events in Sulfolobus acidocaldarius
Abstract: Signal recognition particles are ubiquitous ribonucleoprotein complexes occurring in all domains of life. Archaeal SRPs consist of the SRP RNA and the proteins SRP54, SRP19 and L7Ae. The RNA is usually a linear molecule, however the hyperthermophilic organism Thermoproteus tenax possesses a permuted, intron-containing SRP RNA gene which is processed into a circular SRP RNA. Hence, a permuted SRP RNA gene was introduced into the thermoacidophilic archaeon Sulfolobus acidocaldarius. Furthermore, following the discovery of NAD-capped RNAs in S. acidocaldarius, four Nudix domain-containing proteins constituting potential NAD-decapping enzymes were deleted and the knock-out strains subjected to transcriptomic and metabolomic analyses.