Author

J. Lutkenhaus

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· 5 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:E. coli· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:cell type annotation· 2 Research Focus:chromatin & epigenetic regulation· 2 Approach:genetic perturbation / CRISPR· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1

Frequent Co-Authors

S. Du· 4 shared K.-T. Park· 3 shared H. Gong· 2 shared S. Pichoff· 2 shared D. K. Johnson· 1 shared D. Straume· 1 shared E. V. Koonin· 1 shared J. A. Hermoso· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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4 shared papersMicrobiology

S. Du

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

The essential domain of FtsN triggers cell division by promoting interaction between FtsL and FtsI

K.-T. Park, D. K. Johnson, S. Pichoff, S. Du, J. Lutkenhaus

The paper investigates the role of FtsN's essential domain in bacterial cell division by testing a model of its interaction with FtsL and FtsI using genetic analysis and AlphaFold2.

bioRxiv · May 12, 2023 · PreprintMicrobiology

Widespread PRC barrel proteins play critical roles in archaeal cell division

S. Zhao, K. Makarova, W. Zheng, Y. Liu, L. Zhan, Q. Wan, H. Gong, M. Krupovic, J. Lutkenhaus, X. Chen, E. V. Koonin, S. Du

This study identifies three PRC barrel proteins in Haloferax volcanii essential for archaeal cell division, showing their conservation and role in division across haloarchaea.

bioRxiv · Mar 28, 2023 · PreprintMicrobiology

Cell cycle-dependent recruitment of FtsN to the divisome in Escherichia coli

J. Mannik, S. Pichoff, J. Lutkenhaus, J. Mannik

This study quantifies FtsN recruitment to midcell in E. coli and shows it occurs in two stages, with constriction delayed despite FtsN being essential for division.

bioRxiv · Dec 9, 2021Microbiology

Genetic analysis of the septal peptidoglycan synthase FtsWI complex supports a conserved activation mechanism for SEDS-bPBP complexes

S. Du, Y. Li, H. Gong, R. Zhan, S. Ouyang, K.-T. Park, J. Lutkenhaus

The paper identifies mutations in FtsW and FtsI that reveal the activation mechanism of the SEDS-bPBP complex FtsWI, showing it relies on an interaction between FtsW's ECL4 and FtsI's pedestal domain.

bioRxiv · Jan 21, 2021Microbiology

Essential role for FtsL in activation of septal PG synthesis

K.-T. Park, S. Du, J. Lutkenhaus

This study identifies a region of FtsL critical for activating FtsWI in bacterial cytokinesis, showing FtsL interacts with FtsI to facilitate septal peptidoglycan synthesis.

bioRxiv · Sep 1, 2020Microbiology

Structural characterization of the essential cell division protein FtsE and its interaction with FtsX in Streptococcus pneumoniae

M. Alcorlo, D. Straume, J. Lutkenhaus, L. S. Havarstein, J. A. Hermoso

This paper reports the high-resolution structures of FtsE from Streptococcus pneumoniae in complex with nucleotides, revealing its ATPase activity and structural plasticity essential for FtsX interaction.

bioRxiv · Jun 8, 2020Biochemistry