Lasse Bohl Jenner

Localisation and regulation of the ribosome and protein synthesis


We study the interaction between the eukaryote ribosome and binding partners (membrane proteins / receptors / other ligands) that regulate protein synthesis in order to understand how intra- and extra-cellular signaling is able to influence gene expression as well as how ribosomes are recruited and localized to specific subcellular areas. Control of metazoan gene expression plays a vital role in cell growth, differentiation and development and a strict and precise regulation of the protein synthetic apparatus is required in order to achieve this control.

A comparison of the existing ribosome structures from prokaryotic and eukaryotic organisms shows that the eukaryotic ribosome has a higher degree of complexity than its prokaryotic counterpart. Almost all of the eukaryotic rRNA expansion segments and additional ribosomal proteins are located on the solvent exposed surface, whereas the functional centers within the ribosome show a high degree of conservation between all kingdoms of life. These additional surface elements are thought to constitute docking platforms and binding areas for ribosomal ligands that facilitate the translational regulation needed to generate the advanced cellular organization of different tissue and elaborate body plan that is characteristic of eukaryotic organisms. The focus of our group is to determine structures of the ribosome in complex with these ligands in order to get a detailed picture of the interaction that exists between two such partners.

Our research is generously funded by a Hallas-Møller stipend to Lasse Bohl Jenner from the Novo-Nordisk foundation

Research interests:

  • Signaling pathways involved in regulation of translation
  • Protein synthesis and establishment of long-term memory
  • Recruitment of the ribosome
  • RNAi mechanisms and translational control
  • Spatial and temporal localization of the ribosome and protein synthesis


  • Recombinant expression of proteins (bacteria, yeast, mammalian cells).
  • Purification of proteins from recombinant sources by chromatography.
  • Isolation of ribosomes from various eukaryotic organisms.
  • Analysis of ribosome*ligand complexes (surface plasmon resonance (SRP), isothermal titration calorimetry (ITC)).
  • Functional studies of interaction surfaces (mutagenesis).
  • Structural analysis of macromolecular assemblies (light scattering, small-angle x-ray scattering).
  • High-resolution structure determination (X-ray crystallography).
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