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
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
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
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
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
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
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
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
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
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.