A tRNA modifier at work

Heidelberg, 11 July 2019

Cryo-EM reveals the structure of a piece of cellular machinery with important medical implication.more

Source Article

Dauden MI et al.Molecular basis of tRNA recognition by the Elongator complex. Science Advances. Published online 10 July 2019. DOI: 10.1126/sciadv.aaw2326  DOI: 10.1126/sciadv.aaw2326

More effective insulin thanks to first 3D image

Heidelberg, 24 October 2018

New study reveals how to make therapeutic insulins more effective than they currently are. more

Source Article

Weis, F., et al. The signalling conformation of the insulin receptor ectodomain. Nature Communications, published online 24 October 2018. DOI: 10.1038/s41467-018-06826-6

Pol III enzyme grips DNA and begins reading fast

Heidelberg, 18 January 2018

EMBL researchers uncover how a key enzyme that helps cells make new proteins starts its work. more

Source Article

Vorländer, M. et al. Molecular mechanism of promoter opening by RNA polymerase III, Nature, published online 17 January 2018. DOI: 10.1038/nature25440

New insights into RNA Polymerase I

Heidelberg, 18 November 2016

Cryo EM reconstruction of RNA Polymerase I reveals details of how molecule binds and transcribes DNA. more

Source Article

Tafur L et al., Molecular Structures of Transcribing RNA Polymerase I. Molecular Cell, published online 17 November 2016. doi: 10.1016/j.molcel.2016.11.013

True love

Heidelberg, 11 February 2016

Key proteins involved in gene expression depend on each other when forming a heart in an embryo, but, if left alone, they start to run amok. more

Source Article

Luna-Zurita L et al. Complex Interdependence Regulates Heterotypic Transcription Factor Distribution and Coordinates Cardiogenesis. Cell. 11 February 2016 doi: 10.1016/j.cell.2016.01.004

Pol III: Completing the family album

Heidelberg, 25 November 2015

In a paper published today in Nature, Christoph Müller’s and Carsten Sachse’s groups present the first high-resolution structure of Pol III, achieved with cryo-electron microscopy (cryo-EM) techniques. more

Source Article

Hoffmann et al. Molecular structures of unbound and transcribing RNA polymerase III. Nature 528(7581):231-236. 25 November 2015 doi: 10.1038/nature16143.

Oskar’s structure revealed

Heidelberg, 16 July 2015

The structure of two parts of the Oskar protein, known to be essential for the development of reproductive cells, has been solved by scientists from EMBL Heidelberg. more

Source Article

Jeske, Bordi, Glatt et al. The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase- and RNA-Binding Activities. Cell Rep 16 July 2015. doi: 10.1016/j.celrep.2015.06.055.

Bigger, better, faster

Heidelberg, 23 October 2013

The molecular machine that makes essential components of ribosomes is like a Swiss-army knife, researchers at EMBL Heidelberg and collaborators have found. more

Source Article

Fernández-Tornero, C. et al. Crystal structure of the 14-subunit RNA polymerase I. Nature 502(7473):644–649. doi: 10.1038/nature12636.

Trapped in a ring

Heidelberg, 19 February 2012

A ring-like structure found in a protein complex called ‘Elongator’ provides new clues to its tasks inside the cell and to its role in neurodegenerative diseases. It is the first three-dimensional structure of part of this complex, and was published online today in NSMB. more

Source Article

Glatt, S. et al. The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase. Nat Struct Mol Biol 19(3):314–320. doi: 10.1038/nsmb.2234.

Putting the squeeze on sperm DNA

Heidelberg/Grenoble, 30 September 2009

Scientists at the European Molecular Biology Laboratory (EMBL) in Heidelberg and Grenoble, the Institut de Biologie Structurale (IBS) and the Institut Albert Bonniot, both also in Grenoble, have been studying the secrets of speedy sperm. Their work shows how a protein only found in developing sperm cells, Brdt, directs tight re-packaging of sperm DNA. more

Source Article

Morinière, J. et al. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 461(7264): 664–668. doi: 10.1038/nature08397.