Ralph Krafczyk

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Department of Organic Chemistry, School University, Shanghai 200433, China. E-mai Department of Biology I, Microbiology, Lu Munich, Germany Center for Integrated Protein Science M München, Munich, Germany. E-mail: juerge Structural and Computational Biology Un Germany School of Pharmacy, Wei Fang Medical Uni Institute of Infection and Immunity, Taihe(More)
A previously discovered posttranslational modification strategy - arginine rhamnosylation - is essential for elongation factor P (EF-P) dependent rescue of polyproline stalled ribosomes in clinically relevant species such as Pseudomonas aeruginosa and Neisseria meningitidis. However, almost nothing is known about this new type of N-linked glycosylation. In(More)
The analysis of the function of essential genes in vivo depends on the ability to experimentally modulate levels of their protein products. Current methods to address this are based on transcriptional or post-transcriptional regulation of mRNAs, but approaches based on the exploitation of translation regulation have so far been neglected. Here we describe a(More)
Glycosylation is a universal strategy to posttranslationally modify proteins. The recently discovered arginine rhamnosylation activates the polyproline-specific bacterial translation elongation factor EF-P. EF-P is rhamnosylated on arginine 32 by the glycosyltransferase EarP. However, the enzymatic mechanism remains elusive. In the present study, we solved(More)
a Department of Organic Chemistry, School of Pharmacy, Second Military Medical University, Shanghai 200433, China b Department of Biology I, Microbiology, Ludwig Maximilians-Universität München, Munich, Germany Center for Integrated Protein Science Munich, Ludwig-Maximilians-Universität München, Munich, Germany c Structural and Computational Biology Unit,(More)
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