L. Jenner

ORCID: 0000-0003-3917-8853
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About
Contact & Profiles
Research Areas
  • RNA and protein synthesis mechanisms
  • RNA modifications and cancer
  • RNA Research and Splicing
  • Bacterial Genetics and Biotechnology
  • Genomics and Phylogenetic Studies
  • Toxin Mechanisms and Immunotoxins
  • Bacteriophages and microbial interactions
  • Complement system in diseases
  • Radiopharmaceutical Chemistry and Applications
  • Molecular Biology Techniques and Applications
  • Enzyme Structure and Function
  • Monoclonal and Polyclonal Antibodies Research
  • Peptidase Inhibition and Analysis
  • Viral Infections and Immunology Research
  • Natural product bioactivities and synthesis
  • Neutrino Physics Research
  • Ferrocene Chemistry and Applications
  • Machine Learning in Bioinformatics
  • RNA regulation and disease
  • Statistics Education and Methodologies
  • Prostate Cancer Treatment and Research
  • Porphyrin Metabolism and Disorders
  • Crystallization and Solubility Studies
  • Boron and Carbon Nanomaterials Research
  • Iron Metabolism and Disorders

Inserm
2010-2024

Institut de génétique et de biologie moléculaire et cellulaire
2007-2024

Centre National de la Recherche Scientifique
2010-2024

Integrated Structural Biology Grenoble
2024

Université de Strasbourg
2010-2023

Institut de Biologie Moléculaire et Cellulaire
2005-2021

Aarhus University
1998-2018

Fraunhofer Institute for Interfacial Engineering and Biotechnology
2008

University of Nebraska Medical Center
2008

Max Perutz Labs
2007

A close-up view of the ribosome’s 79 proteins and 5500 RNA nucleotides.

10.1126/science.1212642 article EN Science 2011-11-18

Crystal structures of prokaryotic ribosomes have described in detail the universally conserved core translation mechanism. However, many facets process eukaryotes are not shared with prokaryotes. The crystal structure yeast 80S ribosome determined at 4.15 angstrom resolution reveals higher complexity eukaryotic ribosomes, which 40% larger than their bacterial counterparts. Our model shows how eukaryote-specific elements considerably expand network interactions within and provides insights...

10.1126/science.1194294 article EN Science 2010-11-25

Here we present an X-ray crystallography structure of the clinically relevant tigecycline antibiotic bound to 70S ribosome. Our structural and biochemical analysis indicate that enhanced potency results from a stacking interaction with nucleobase C1054 within decoding site Single-molecule fluorescence resonance energy transfer studies reveal that, during decoding, inhibits initial codon recognition step tRNA accommodation prevents rescue by tetracycline-resistance protein TetM.

10.1073/pnas.1216691110 article EN Proceedings of the National Academy of Sciences 2013-02-19

Abstract Translation of the genetic code into proteins is realized through repetitions synchronous translocation messenger RNA (mRNA) and transfer RNAs (tRNA) ribosome. In eukaryotes ensured by elongation factor 2 (eEF2), which catalyses process actively contributes to its accuracy 1 . Although numerous studies point critical roles for both conserved eukaryotic posttranslational modification diphthamide in eEF2 tRNA modifications supporting translocation, detailed molecular mechanisms...

10.1038/s41586-021-04131-9 article EN cc-by Nature 2021-12-01

The ribosome of Thermus thermophilus was cocrystallized with initiator transfer RNA (tRNA) and a structured messenger (mRNA) carrying translational operator. path the mRNA defined at 5.5 angstroms resolution by comparing it either crystal structure same ribosomal complex lacking or an unstructured mRNA. A precise environment positions operator stem-loop perpendicular to surface on platform 30S subunit. binding tRNA occurs unoccupied exit site, which is expected for initiation complex....

10.1126/science.1105639 article EN Science 2005-03-31

The emergence of drug-resistant tuberculosis has created an urgent need for new anti-tubercular agents. Here, we report the discovery a series macrolides called sequanamycins with outstanding in vitro and vivo activity against Mycobacterium (Mtb). Sequanamycins are bacterial ribosome inhibitors that interact similar manner to classic like erythromycin clarithromycin, but binding characteristics allow them overcome inherent macrolide resistance Mtb. Structures bound were used optimize...

10.1016/j.cell.2023.01.043 article EN cc-by Cell 2023-02-23

Abstract In response to cellular stresses bacteria conserve energy by dimerization of ribosomes into inactive hibernating 100S ribosome particles. Ribosome in Thermus thermophilus is facilitated hibernation-promoting factor ( Tt HPF). this study we demonstrate high sensitivity formation the levels HPF and show that a 1:1 ratio leads optimal dimerization. We report structures T. determined cryo-electron microscopy average resolutions 4.13 Å 4.57 Å. addition, present 3.28 high-resolution...

10.1038/s41467-018-06724-x article EN cc-by Nature Communications 2018-10-03

The estimation of the bulk-solvent contribution to diffraction a macromolecular crystal makes use solvent mask which delimits regions in crystal. It is shown that way this usually defined CNS contains bias can lead absurd results case very large structures, where calculations only be made on relatively coarse grids. A modified procedure described and applied 70S ribosome data at 5.5 Å resolution. B factor affecting bulk also discussed. Even high widely variable atomic factors, it seems...

10.1107/s0907444905019591 article EN Acta Crystallographica Section D Biological Crystallography 2005-08-16

Translation initiation factor 2 (IF2) is involved in the early steps of bacterial protein synthesis. It promotes stabilization initiator tRNA on 30S complex (IC) and triggers GTP hydrolysis upon ribosomal subunit joining. While structure an archaeal homologue (a/eIF5B) known, there are significant sequence functional differences eubacterial IF2, while trimeric eukaryotic IF2 completely unrelated. Here, crystal apo core from Thermus thermophilus has been determined by MAD phasing structures...

10.1107/s0907444913006422 article EN cc-by Acta Crystallographica Section D Biological Crystallography 2013-04-22
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