4 research departments
750 employees
45 nationalities
55 research teams
16 ERC laureates
260 publications per year
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Fondation universite de Strasbourg
Wednesday, April 24th 2019 - 10 a.m.
Pr Anton Zilman

Nuclear Pore Complex: simple biophysics of a complex biomachine

Friday, April 26th 2019 - 11 a.m.
Pr Julie Ahringer

Genome architecture and regulation

Palmarès prix de thèse SBS : Prix de la Fondation Unistra 2017 Société de Biologie de Strasbourg : Patrick LAURETTE

The manufacture of multi-protein complexes: a new assembly method unveiled

Simultaneous (on the left) and sequential co-translation (on the right)

April 15, 2019

The assembly of proteins into large macromolecular complexes is essential to the viability of cells. However, since genes encoding proteins that constitute such multiprotein complexes are dispersed in the eukaryotic genome, it is difficult to understand how these subunits can assemble. In this study, Laszlo Tora's team at the IGBMC (CNRS/Inserm/Université de Strasbourg) determined a pathway for assembling mammalian transcription complexes (TFIID, SAGA and TREX-2), each composed of a large number of subunits. According to their observations, complex assembly would be carried out during the synthesis of the proteins that constitute these complexes. These results are published in Nature Communications on April 15, 2019. 

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A new therapeutic strategy for myotubular myopathy

Cross sections of muscles. Left the normal muscle fibers, in the middle those of a diseased mouse and on the right those of a diseased mouse overexpressing Bin1

March 20, 2019

After identifying amphiphysin 2 as a potential therapeutic target in some congenital myopathies, researchers in Jocelyn Laporte's team at the IGBMC (CNRS/Inserm/Université de Strasbourg) were able to specifically modulate the level of this molecule and to reduce all signs of a severe form of myopathy. These results, published on March 20, 2019, in the journal Science translational medicine, offer new therapeutic perspectives for these myopathies.


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Identification of a new partnership in gene expression regulation

On the left, compact chromatin. On the right, decondensed chromatin following the interaction of mutated TFIIH with the GCN5 enzyme.

March 20, 2019

Patients with a combined form of xeroderma pigmentosum and Cockayne syndrome have a wide range of clinical characteristics, including photosensitivity of the skin, predisposition to cancer and developmental disorders. At the origin of this rare genetic disease, a mutation of a subunit of the gene encoding TFIIH that plays a key role both in gene transcription and in gene repair. By studying patients' cells, researchers from Frédéric Coin's team at the IGBMC (CNRS/Inserm/Unistra) showed that the interaction of the TFIIH complex with the GCN5 enzyme leads to an increase in the enzymatic activity of GCN5, resulting in an uncontrolled remodelling of the chromatin and an overexpression of a large number of genes that may cause certain symptoms in patients.These results are published on March 20, 2019 in the journal Nature Communication.


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