This release is available in German.
FRANKFURT. A newly synthesized protein is as fragile as a newborn baby. It could never fold into its correct three dimensional structure if it was not protected by chaperones within the densely populated cytosol. In case of membrane proteins chaperones do not only pre-vent their aggregation, but also escort them to their destination and aid in membrane insertion. The underlying molecular mechanism of how a certain family of membrane proteins is targeted and inserted into membranes has now been resolved by an international research team with participation of the Goethe University Frankfurt. These proteins are anchored within the membrane via a single helix and thus are called "tail-anchored" (TA) proteins.
The key for proper protein sorting are signal sequences which are decoded by chaperones. As soon as they - together with their "foster child" - arrive at their destination the interaction with a specific receptor within the target membrane initiates membrane insertion. Protein components responsible for the insertion of TA proteins have recently been identified. The molecular mechanisms of how these sorting systems work, however, were not known so far.
In this interdisciplinary study, that will be released in the current "online" issue of "Science", the research groups of Prof.Volker Dtsch (Goethe University Frankfurt), Prof. Irmgard Sinning (Heidelberg University Biochemistry Center) and Prof. Vlad Denic (Harvard University (USA)) were able to solve the question by a combination of diverse methods such as X-Ray Crystallography and NMR-Spectroscopy as well as biochemical and cell-biological approaches.
In detailed biophysical studies Volker Dtschs research group showed that the central cha-peron of the responsible protein complex, called Get3, regulates both binding to TA proteins within the cytoso
|Contact: Prof. Volker Dtsch|
Goethe University Frankfurt