Author

R. Krafczyk

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:E. coli· 2 Assay:proteomics· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

J. Lassak· 2 shared K. Jung· 2 shared P. Kielkowski· 2 shared A. Hoffmann-Roeder· 1 shared A. Imhof· 1 shared A. K. Jha· 1 shared A. M. Sieber· 1 shared A. Schaepers· 1 shared

Activity by Year

2017-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersMicrobiology

J. Lassak

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

EF-P and its paralog EfpL (YeiP) differentially control translation of proline containing sequences

A. M. Sieber, M. Parr, J. von Ehr, K. Dhamotharan, P. Kielkowski, T. Brewer, A. Schaepers, R. Krafczyk, F. Qi, A. Schlundt, D. Frishman, J. Lassak

This study identifies EfpL as a ribosome rescue factor that senses cellular metabolic state, complementing EF-P in proline-containing sequence translation.

bioRxiv · Apr 15, 2024Microbiology

Decrypting the functional design of unmodified translation elongation factor P

U. Tomasiunaite, P. Kielkowski, R. Krafczyk, I. Forne, A. Imhof, K. Jung

This study identifies unmodified EF-P variants from Rhodomicrobium vannielii that restore function in E. coli lacking EF-P modifications, revealing design principles for polyproline synthesis.

bioRxiv · Sep 18, 2023Microbiology

Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P

R. Krafczyk, J. Macosek, D. Gast, S. Wunder, P. K. A. Jagtap, P. Mitra, A. K. Jha, J. Rohr, A. Hoffmann-Roeder, K. Jung, J. Hennig, J. Lassak

The paper determines the crystal structure of EarP, revealing its mechanism for arginine glycosylation of EF-P and its role in bacterial pathogenicity.

bioRxiv · Mar 13, 2017Biochemistry