Author

H. Feddersen

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Microbiology· 4

Signature Assays, Organisms & Methods

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Organism:bacteria (other)· 3 Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Approach:statistical model· 2 Research Focus:chromatin & epigenetic regulation· 1 Assay:fluorescence / live-cell microscopy· 1 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1

Frequent Co-Authors

M. Bramkamp· 4 shared G. Giacomelli· 2 shared C. Dyckmans· 1 shared C. K. Das· 1 shared D. Trojanowski· 1 shared E. Frey· 1 shared F. Altegoer· 1 shared G. Bange· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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4 shared papersMicrobiology

M. Bramkamp

Mutual co-authors in cluster

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4 papers

Recent·Most cited

Membrane Binding Controls the ATPase Cycle and Localization of MinD in Bacillus subtilis

H. Feddersen, C. Dyckmans, M. Bramkamp

This study shows that membrane binding activates MinD ATPase activity and regulates its localization in B. subtilis, with dynamics explained by binding kinetics without requiring additional proteins.

bioRxiv · Jul 8, 2024Microbiology

The CTPase activity of ParB acts as a timing mechanism to control the dynamics and function of prokaryotic DNA partition complexes

M. Osorio-Valeriano, F. Altegoer, C. K. Das, W. Steinchen, G. Panis, L. Connolley, G. Giacomelli, H. Feddersen, L. Corrales-Guerrero, P. Giammarinaro, J. Hanssmann, M. Bramkamp, P. H. Viollier, S. Murray, L. V. Schäfer, , M. Thanbichler

This study identifies how ParB's CTPase activity regulates DNA partition complex dynamics and function by controlling clamp sliding time and spreading.

bioRxiv · May 5, 2021Microbiology

Dynamics of the Bacillus subtilis Min system

H. Feddersen, L. Wuerthner, E. Frey, M. Bramkamp

This study shows that the Min system in Bacillus subtilis dynamically localizes to active division sites, forming clusters, and provides physical modeling to explain its behavior.

bioRxiv · Apr 29, 2020Microbiology

Lsr2 is a nucleoid-associated protein that exerts pleiotropic effects on mycobacterial cellular processes

M. Kolodziej, D. Trojanowski, K. Bury, J. Holowka, M. Pasciak, W. Matysik, H. Kakolewska, H. Feddersen, G. Giacomelli, M. Bramkamp, I. Konieczny, J. Zakrzewska-Czerwinska

This study shows that Lsr2 is essential for mycobacterial chromosome structure and cell envelope properties, with implications for drug development.

bioRxiv · Apr 27, 2020 · PreprintMicrobiology