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Switching the Post-Translational Modification of Elongation Factor P

45 Pages Posted: 8 Nov 2018 Sneak Peek Status: Under Review

See all articles by Wolfram Volkwein

Wolfram Volkwein

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Ralph Krafczyk

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Pravin Kumar Ankush Jagtap

European Molecular Biology Laboratory - Structural and Computational Biology Unit

Marina Parr

Technische Universität München (TUM) - Department of Bioinformatics

Elena Mankina

Technische Universität München (TUM) - Department of Bioinformatics

Jakub Macošek

European Molecular Biology Laboratory - Structural and Computational Biology Unit

Zhenghuan Guo

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Maximilian Josef Ludwig Johannes Fürst

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Miriam Pfab

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Dmitrij Frishman

Saint Petersburg State Polytechnical University

Janosch Hennig

European Molecular Biology Laboratory - Structural and Computational Biology Unit

Kirsten Jung

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Jürgen Lassak

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

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Abstract

Tripeptides with two consecutive prolines are the shortest and most frequent sequences causing ribosome stalling. The bacterial translation elongation factor P (EF-P) relieves the arrest, allowing protein biosynthesis to continue. A seven amino acids long loop between beta-strands β3/β4 is crucial for EF-P function and is modified at its tip by lysylation of lysine or rhamnosylation of arginine. Phylogenetic analyses unveiled an invariant proline in the -2 position of the modification site in EF Ps that utilize lysine modifications such as Escherichia coli. Bacteria with arginine modifications such as Pseudomonas putida have selected against it. Focusing on the EF-Ps from these two model organisms we demonstrate the importance of the β3/β4 loop composition for functionalization with chemically distinct modifications. Ultimately we show that amino acid changes in E. coli EF P are needed for switching the activation strategy from lysylation to rhamnosylation.

Suggested Citation

Volkwein, Wolfram and Krafczyk, Ralph and Jagtap, Pravin Kumar Ankush and Parr, Marina and Mankina, Elena and Macošek, Jakub and Guo, Zhenghuan and Fürst, Maximilian Josef Ludwig Johannes and Pfab, Miriam and Frishman, Dmitrij and Hennig, Janosch and Jung, Kirsten and Lassak, Jürgen, Switching the Post-Translational Modification of Elongation Factor P (November 7, 2018). Available at SSRN: https://ssrn.com/abstract=3280239 or http://dx.doi.org/10.2139/ssrn.3280239
This is a paper under consideration at Cell Press and has not been peer-reviewed.

Wolfram Volkwein

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Martinsried
Germany

Ralph Krafczyk

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Martinsried
Germany

Pravin Kumar Ankush Jagtap

European Molecular Biology Laboratory - Structural and Computational Biology Unit

Heidelberg, 69117
Germany

Marina Parr

Technische Universität München (TUM) - Department of Bioinformatics

Arcisstrasse 21
Munich, 80333
Germany

Elena Mankina

Technische Universität München (TUM) - Department of Bioinformatics

Arcisstrasse 21
Munich, 80333
Germany

Jakub Macošek

European Molecular Biology Laboratory - Structural and Computational Biology Unit

Heidelberg, 69117
Germany

Zhenghuan Guo

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Martinsried
Germany

Maximilian Josef Ludwig Johannes Fürst

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Martinsried
Germany

Miriam Pfab

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM)

Martinsried
Germany

Dmitrij Frishman

Saint Petersburg State Polytechnical University

St.Petersburg, 195251,
Russia

Janosch Hennig

European Molecular Biology Laboratory - Structural and Computational Biology Unit

Heidelberg, 69117
Germany

Kirsten Jung

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM) ( email )

Martinsried
Germany

Jürgen Lassak (Contact Author)

Ludwig Maximilian University of Munich - Munich Center for Integrated Protein Science (CiPSM) ( email )

Martinsried
Germany

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