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.