Regulation of protein secretion by the signal recognition particle and its receptor
FP4 — Training and Mobility of Researchers
- Duration
- 1996-09-01 → 2001-08-31
- EU contribution
- —
- Participants
- 9
- Scheme
- —
Lines connect the coordinator with its partners. CORDIS does not always give exact coordinates for projects before 2014. These points are placed at city or country level.
Project objective
The proposed network comprises nine laboratories in seven European countries. All participating laboratories are already actively engaged in ribonucleoprotein complex which mediates targeting of secretory proteins research on structural and/or functional aspects of the signal recognition to the translocation apparatus in the inner membrane of bacteria or the endoplasmic reticulum membrane of eukaryotes. We propose to combine particle with expertise ranging from cell biology through biochemistry to structural and functional methods on both eukaryotic (mammalian, X-ray crystallography. This multi-disciplinary context will be an ideal chlroplast) and prokaryotic (E. coli and Mycoplasma) systems in a framework for the training of the nine post-doctoral fellows which it is multi-disciplinary approach to advance understanding of the mechanism and planned to recruit (one for each network member). In each case, the new recruits will join laboratories in which the participation of other young regulation of this important cellular process. In a field which is almost devoid of high resolution structural information, a major objective will scientists (PhD students, post-doctoral fellows) is high. Furthermore, be structure determination of components of the signal recognition several of the network laboratories are very recently established independent groups ( including one from a less favoured region). These particle and its receptor. We will initially focus the structural work on groups will particularly benefit from participation in the network which (a) the signal sequence binding protein SRP54 and its bacterial also includes more senior groups, well established in the field of protein homologues, secretion. (b) the Alu-domain of mammalian SRP which is responsible for elongation arrest prior to membrane docking and (c) the GTPase domains of SRP54 and the SRP receptor. These structural studies, carried out by three of the network groups, will both benefit and depend on continued functional studies by the other six groups. The major objectives of these studies will be (a) elucidation of SRP-ribosome interactions responsible for signal-dependent elongation arrest (b) identification of GTP-dependent steps of SRP mediated targeting and whether regulation of these steps occurs via GTPase activating or nucleotide exchange factors, (c) elucidation of the interaction between the SRP mediated targeting pathway and the general secretion pathway in E. coli.
Original text from CORDIS.
Participants
- EUROPEAN MOLECULAR BIOLOGY LABORATORY · GRENOBLECoordinatorFrance
- EUROPEAN MOLECULAR BIOLOGY LABORATORY · HEIDELBERGGermany
- FOUNDATION FOR RESEARCH AND TECHNOLOGY - HELLAS · HERAKLIONCity levelGreece
- GOETEBORG UNIVERSITY · GOETEBORGSweden
- RUPRECHT-KARLS-UNIVERSITAET HEIDELBERG · HEIDELBERGGermany
- UNIVERSITY OF GENEVA · GENEVESwitzerland
- UNIVERSITY OF MANCHESTER · MANCHESTERUnited Kingdom
- UNIVERSITY OF UMEAA · UMEAASweden
- VRIJE UNIVERSITEIT AMSTERDAM · AMSTERDAMNetherlands
Links
Data: CORDIS, © European Union
