Graduate Students Mini-Symposium III 2022
Graduate Students Mini-Symposium
- Date: May 16, 2022
- Time: 04:00 PM (Local Time Germany)
- Location: Online
- Host: IMPRS
- Contact: email@example.com
16:00 h Maren Nattermann, AG Erb
“A short cascade for the reduction of formate to formaldehyde"
carbon-neutral bio-economy relies on the efficient recapture of carbon dioxide
from the atmosphere and its conversion into value-added product. In this
context, formic acid is proposed as a convenient storage form, easily produced
from carbon dioxide by electrochemical hydrogenation. A remaining challenge,
however, is the biological availability of formate, which is not easily
channeled into the central metabolism of most platform organisms. One solution
is the conversion of formate to formaldehyde, a compound that is much more
metabolically available. Here, we demonstrate a two-enzyme cascade via formyl
phosphate, consisting of a promiscuous formate kinase and formyl phosphate
16:30 h Tom Kropp, AG Brune
"Diversity and host specificity of the association between Trichonympha flagellates and their bacterial symbionts"
In termites symbiotic flagellates play a major role in symbiotic digestion. These flagellates are associated with a variety of prokaryotic ecto- and endosymbiotic bacteria that often have strict host-specific colonization patterns. The evolutionary history of these associations is not clear. We analyzed the prokaryotic community composition associated with picked Trichonympha cells to identify patterns of cospeciation. We could show that Trichonympha from Cluster II do not share a major bacterial symbiont like Ancillula trichonymphae or Endomicrobium trichonymphae instead only Trichonympha from Incisitermes spp. share Ancillula trichonymphae and other Trichonympha lineages from Cluster II are associated with a variety of bacteria.
17:00 h Memduha Muratoglu, AG Sogaard-Andersen
"Stability & dynamics of the type IVa pilus machine"
The type IVa pilus machine (T4aPM) drives the T4aP extension/retraction cycles and is the prototype of a large family of prokaryotic cell envelope-spanning macromolecular complexes involved in biofilm formation, motility, protein secretion, adhesion and DNA uptake. The T4aPM is composed of 15 proteins in multiple copies. The overall structure of the T4aPM is known while less is known about its mode of action and the dynamics of its individual components. Here, we used Fluorescence recovery after photobleaching (FRAP) to address these questions. Our results support different exchange rates for individual components. We will discuss how these findings inform our understanding of the T4aPM.