Jürgen Lassak

Jürgen Lassak
Ludwig-Maximilians-University of Munich | LMU · Division of Microbiology

PD Dr.

About

96
Publications
14,415
Reads
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1,711
Citations
Citations since 2017
59 Research Items
1205 Citations
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2017201820192020202120222023050100150200
2017201820192020202120222023050100150200
2017201820192020202120222023050100150200
Additional affiliations
August 2019 - March 2021
Ludwig-Maximilians-Universität München
Position
  • Professor (Associate)
Description
  • * Translational stress response * Prokaryotic glycobiology & posttranslational regulation * Synthetic biology
March 2018 - present
Ludwig-Maximilians-Universität München
Position
  • Privatdozent
Description
  • Prokaryotic Glycobiology & Posttranslational Regulation
April 2015 - present
Ludwig-Maximilians-Universität München
Position
  • Group Leader
Education
June 2015 - February 2018
Ludwig-Maximilians-University of Munich (Habilitation)
Field of study
  • Microbiology
September 2007 - December 2010
Philipps University Marburg (PhD Thesis)
Field of study
  • Microbiology
October 1999 - April 2005
Eberhard Karls Universität Tübingen (Diploma)
Field of study
  • Biology

Publications

Publications (96)
Article
Full-text available
Ribosome stalling at polyproline stretches is common and fundamental. In bacteria, translation elongation factor P (EF-P) rescues such stalled ribosomes, but only when it is post-translationally activated. In Escherichia coli, activation of EF-P is achieved by (R)-beta-lysinylation and hydroxylation of a conserved lysine. Here we have unveiled a ma...
Article
Full-text available
Thermal food processing leads to the formation of advanced glycation end products (AGE) such as Nε‐carboxymethyllysine (CML). Accordingly, these non‐canonical amino acids are an important part of the human diet. However, CML is only partially decomposed by our gut microbiota and up to 30% are excreted via feces and, hence, enter the environment. In...
Article
Full-text available
Among the 22 proteinogenic amino acids, lysine sticks out due to its unparalleled chemical diversity of post-translational modifications. This results in a wide range of possibilities to influence protein function and hence modulate cellular physiology. Concomitantly, lysine derivatives form a metabolic reservoir that can confer selective advantage...
Article
Full-text available
l-Rhamnose is an important monosaccharide both as nutrient source and as building block in prokaryotic glycoproteins and glycolipids. Generation of those composite molecules requires activated precursors being provided e. g. in form of nucleotide sugars such as dTDP-β-l-rhamnose (dTDP-l-Rha). dTDP-l-Rha is synthesized in a conserved 4-step reaction...
Article
Full-text available
The speed of mRNA translation depends in part on the amino acid to be incorporated into the nascent chain. Peptide bond formation is especially slow with proline and two adjacent prolines can even cause ribosome stalling. While previous studies focused on how the amino acid context of a Pro-Pro motif determines the stalling strength, we extend this...
Article
Full-text available
Thermally processed food is an important part of the human diet. Heat-treatment, however, promotes the formation of so-called Amadori rearrangement products, such as fructoselysine. The gut microbiota including Escherichia coli can utilize these compounds as a nutrient source. While the degradation route for fructoselysine is well described, regula...
Article
Full-text available
For canonical asparagine glycosylation, the primary amino acid sequence that directs glycosylation at specific asparagine residues is well-established. Here we reveal that a recently discovered bacterial enzyme EarP, that transfers rhamnose to a specific arginine residue in its acceptor protein EF-P, specifically recognizes a β-hairpin loop. Notabl...
Preprint
Full-text available
Protein N-glycosylation is ubiquitously present in all domains of life, and confers a plethora of functions to the protein including increased solubility, protection from degradation, interaction with receptors, and activation for function. For canonical asparagine glycosylation, the recognition sequence that directs glycosylation at specific aspar...
Article
Full-text available
Article
Despite its potential importance for bacterial virulence, protein rhamnosylation has not yet been sufficiently studied. Specific anti-SerRha, anti-ThrRha and anti-AsnRha antibodies allowed the identification of previously unknown monorhamnosylated proteins in cytosol and membrane fractions of bacterial cell lysates. Mapping of the complete rhamnopr...
Article
Acid resistance is an important property for bacteria, such as Escherichia coli , to survive acidic environments like the human gastrointestinal tract. E. coli possesses both passive and inducible acid resistance systems to counteract acidic environments. Thus, E. coli evolved sophisticated signaling systems to sense and appropriately respond to en...
Article
Full-text available
Canocically, tRNA synthetases charge tRNAs. However, the lysyl-tRNA synthetase paralog EpmA catalyzes the attachment of (R)-β-lysine to the ε-amino group of lysine 34 of the translation elongation factor P (EF-P) in Escherichia coli. This modification is essential for EF-P-mediated translational rescue of ribosomes stalled at consecutive prolines....
Preprint
Full-text available
Thermally processed food is an important part of the human diet. Heat-treatment, however, promotes the formation of so-called Amadori rearrangement products (ARPs), such as fructoselysine. The gut microbiota including Escherichia coli can utilize these compounds as a nutrient source. While the degradation route for fructoselysine is well described,...
Article
Full-text available
Post-translational modifications (PTM) are the evolutionary solution to challenge and extend the boundaries of genetically predetermined proteomic diversity. Since PTMs are highly dynamic, they also hold an enormous regulatory potential. It is therefore not surprising that out of the 20 proteinogenic amino acids, 15 can be post-translationally modi...
Article
Full-text available
Tripeptides with two consecutive prolines are the shortest and most frequent sequences causing ribosome stalling. The bacterial translation elongation factor P (EF-P) relieves this arrest, allowing protein biosynthesis to continue. A seven amino acids long loop between beta-strands β3/β4 is crucial for EF-P function and modified at its tip by lysyl...
Preprint
Full-text available
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 lys...
Article
Full-text available
Bei der Produktion der bereits veröffentlichten Originalversion des Artikels ist ein Fehler in der Abbildung entstanden: Das Strukturmodell im Ausschnitt rechts hat gefehlt. Anbei finden Sie die korrigierte Version. Wir entschuldigen uns für den Fehler und für alle dadurch eventuell entstandenen Unannehmlichkeiten. Die Online-Version des Originalar...
Article
Full-text available
Every living cell possesses numerous transmembrane signalling systems that receive chemical and physical stimuli from the environment and transduce this information into an intracellular signal that triggers some form of cellular response. As unicellular organisms, bacteria require these systems for survival in rapidly changing environments. The re...
Thesis
Full-text available
Bei der Synthese von mindestens zwei aufeinanderfolgenden Prolinen kommt es zu einem Translationsarrest. Um diesen aufzuheben, haben Bakterien einen spezialisierten Translationsfaktor EF-P evolviert, der dem eukaryotischen / archaealen IF-5A ortholog und funktionsäquivalent ist. In der vorliegenden Arbeit werden die mehr als 40 Jahre Forschung zu I...
Article
Full-text available
Translation of consecutive prolines causes ribosome stalling, which is alleviated but cannot be fully compensated by the elongation factor P. However, the presence of polyproline motifs in about one third of the E. coli proteins underlines their potential functional importance, which remains largely unexplored. We conducted an evolutionary analysis...
Data
Occurrence of polyproline motifs is lower than the random level. The histogram shows the numbers of motifs found in 1,000 sets of random sequences and the blue line shows the number of motifs found in real sequences. The results for 42 E. coli strains (except for E. coli K-12 MG1655) are shown. The OMA id and fold change for each strain are shown i...
Data
List of all 43 E. coli strains used in this study. (XLSX)
Data
Occurrences of polyproline motifs in the core/accessory proteome in the 43 E. coli strains. The OMA id of each strain is shown on the x-axis. For mapping OMA ids to the names of strains, please see S2 Table. Fold changes for the core proteome: mean 0.76, standard deviation 0.003. Fold changes for the accessory proteome: mean 0.85. standard deviatio...
Data
Motif classification. (XLSX)
Data
Numbers of E. coli proteins with 1, 2 and >2 polyproline motifs. (PDF)
Data
Numbers of polyproline motifs negatively correlate with the strength of the ribosome stalling effect. The results for 42 E. coli strains (except for E. coli K-12 MG1655) are shown. The OMA id of each strain is shown in the panel title. For mapping OMA ids to names of strains, please see S2 Table. All the differences are significant according to Man...
Data
Occurrence of polyproline motifs in the core proteome is lower than that in the accessory proteome. The results for 42 E. coli strains (except for E. coli K-12 MG1655) are shown. The OMA id of each strain is shown in the panel title. For mapping OMA ids to names of strains, please see S2 Table. All the differences are significant according to Mann-...
Data
Occurrence of polyproline motifs is correlated with the number of proteins in the proteomes. Pearson’s r = 0.68, p-value = 4.82e-7. (PDF)
Data
Histogram of the TMH length. (PDF)
Data
Occurrence of polyproline motifs in B. subtilis is lower than the random level. The histogram shows the numbers of motifs found in 1,000 sets of random sequences and the blue line shows the number of motifs found in real sequences. The name and fold change of each strain are shown in the panel title. The proteomes of the 4 B. subtilis strains inclu...
Data
The distribution of polyproline motifs in B. subtilis is qualitatively similar to E. coli. The strain 168 were used as a reference strain of B. subtilis. (A) Occurrence of polyproline motifs in the first 50 residues is higher than elsewhere in the protein sequence (Mann-Whitney-Wilcoxon test, p-value < 2.2e-16; fold change 0.82 vs 0.73). Error bars...
Data
The list of 2,115 polyproline motifs identified in E. coli K-12 MG1655. (XLSX)
Data
Classification of the effect amino acids at position X(-2), X(-1) and X(+1) exert on ribosomal stalling strength. (PDF)
Data
Rules for the prediction of ribosomal stalling strength induced by a X(-2)X(-1)-nP-X(+1) motif. (PDF)
Data
Matching the predicted stalling strength of polyproline motifs with the ribosome profiling data from C. J. Woolstenhulme [Cell Rep 11:13–21, 2015]. (XLSX)
Article
Full-text available
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, w...
Article
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 translational regulation have so far been neglected. Here we...
Article
Full-text available
The transmembrane DNA-binding protein CadC of E. coli, a representative of the ToxR-like receptor family, combines input and effector domains for signal sensing and transcriptional activation, respectively, in a single protein, thus representing one of the simplest signalling systems. At acidic pH in a lysine-rich environment, CadC activates the tr...
Preprint
Glycosylation is a universal strategy to post-translationally 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,...
Article
Full-text available
A previously discovered posttranslational modification strategy – arginine rhamnosylation – is essential for EF-P dependent rescue of polyproline stalled ribosomes in clinical relevant species such as Pseudomonas aeruginosa and Neisseria meningitidis. However, almost nothing is known about this new type of N-linked glycosylation. In the present stu...
Article
Full-text available
Phages are bacteria targeting viruses and represent the most abundant biological entities on earth. Marine environments are exceptionally rich in bacteriophages, harboring a total of 4x1030 viruses. Nevertheless, marine phages remain poorly characterized. Here we describe the identification of intact prophage sequences in the genome of the marine γ...
Data
Relative mean coverage of sequencing reads of predicted V. campbellii ATCC BAA-1116 prophages. (PDF)
Data
Effect of mitomycin C on growth of V. campbellii. Mitomycin C (final concentration of 1 μg/ml, indicated in green) and DMSO (control, indicated in red) was added to the culture during the exponential growth phase for 0.5 h (time point I). Then cells were washed twice in fresh AB medium. Phage lysate was prepared at time point P. Cell densities were...
Article
Full-text available
Die Translation eines Proteins stoppt, wenn drei aufeinanderfolgende Proline in die Polypetidkette eingebaut werden müssen. Dieser Translationsstopp wird durch die Aktivität des Elongationsfaktors P (EF-P) aufgehoben. EF-P und die orthologen Proteine IF-5A in Eukaryoten und Archaeen sind in allen Lebewesen vorhanden und für die effiziente Synthese...
Article
Translation of polyproline proteins leads to translation arrest. To overcome this ribosome stalling effect, bacteria depend on a specialized translation elongation factor P (EF-P), being orthologous and functional identical to eukaryotic/archaeal elongation factor e/aIF-5A (recently renamed "EF5"). EF-P binds to the stalled ribosome between the pep...
Article
Full-text available
In Escherichia coli, detoxification of methylglyoxal (MG) requires glyoxalases I and II. Glyoxalase I (gloA/GlxI) isomerizes the hemithioacetal, formed spontaneously from MG and glutathione (GSH) to S-lactoylglutathione (SLG), which is hydrolyzed by glyoxalase II (gloB/GlxII) to lactate and GSH. YcbL from Salmonella enterica serovar Typhimurium is...
Article
Full-text available
Bacterial ribosomes stall on polyproline stretches and require the elongation factor P (EF-P) to relieve the arrest. Yet it remains unclear why evolution has favored the development of EF-P rather than selecting against the occurrence of polyproline stretches in proteins. We have discovered that only a single polyproline stretch is invariant across...
Article
Full-text available
β-galactosidase encoded by lacZ remains a popular reporter enzyme. Here, we present a convenient tool box to facilitate rapid construction of reporter lacZ fusions. The first tool enables the simple generation of chromosomally encoded reporters within the Escherichia coli lac operon using Red®/ET® recombination. The second tool allows the introduct...
Article
Full-text available
The polymerization of amino acids into proteins occurs on ribosomes, with the rate influenced by the amino acids being polymerized. The imino acid proline is a poor donor and acceptor for peptide-bond formation, such that translational stalling occurs when three or more consecutive prolines (PPP) are encountered by the ribosome. In bacteria, stalli...
Article
Throughout their life, bacteria need to sense and respond to environmental stress. Thus, such stress responses can require dramatic cellular reprogramming, both at the transcriptional as well as the translational level. This review focuses on the protein factors that interact with the bacterial translational apparatus in order to respond to and cop...
Article
Full-text available
During translation, amino acids are not incorporated into the growing nascent polypeptide chain at the same rates; in fact, distinct amino acid sequences, such as a stretch of three or more consecutive prolines, can cause translation to stop. We discovered that ribosomes stalled on these polyproline stretches are rescued by the translation elongati...
Article
Full-text available
Significance During protein synthesis, ribosomes catalyze peptide-bond formation between amino acids with differing efficiency. We show that two or more consecutive prolines induce ribosome stalling, and that stalling strength is influenced by the amino acid preceding and following the prolines. In bacteria, the elongation factor EF-P efficiently r...
Article
Full-text available
Translation elongation factor P (EF-P) is critical for virulence in bacteria. EF-P is present in all bacteria and orthologous to archaeal and eukaryotic initiation factor 5A, yet the biological function has so far remained enigmatic. Here, we demonstrate that EF-P is an elongation factor that enhances translation of polyproline-containing proteins:...
Article
Full-text available
In all species of the genus Shewanella, the redox-sensing Arc two-component system consists of the response regulator ArcA, the sensor kinase ArcS, and the separate phosphotransfer protein HptA. Compared to its counterpart ArcB in Escherichia coli, ArcS has a significantly different domain structure. Resequencing and reannotation revealed that in t...