CRYOTRANSLATION

High Resolution cryo-EM Analysis of Ribosome-associated Functions

 Coordinatore LUDWIG-MAXIMILIANS-UNIVERSITAET MUENCHEN 

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 Nazionalità Coordinatore Germany [DE]
 Totale costo 2˙995˙640 €
 EC contributo 2˙995˙640 €
 Programma FP7-IDEAS-ERC
Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call ERC-2011-ADG_20110310
 Funding Scheme ERC-AG
 Anno di inizio 2012
 Periodo (anno-mese-giorno) 2012-05-01   -   2017-04-30

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    LUDWIG-MAXIMILIANS-UNIVERSITAET MUENCHEN

 Organization address address: GESCHWISTER SCHOLL PLATZ 1
city: MUENCHEN
postcode: 80539

contact info
Titolo: Mr.
Nome: Brice
Cognome: Rousseau
Email: send email
Telefono: +49 89 2180 72274
Fax: +49 89 2180 2985

DE (MUENCHEN) hostInstitution 2˙995˙640.00
2    LUDWIG-MAXIMILIANS-UNIVERSITAET MUENCHEN

 Organization address address: GESCHWISTER SCHOLL PLATZ 1
city: MUENCHEN
postcode: 80539

contact info
Titolo: Prof.
Nome: Roland
Cognome: Beckmann
Email: send email
Telefono: +49 89 2180 76900
Fax: +49 89 3280 76945

DE (MUENCHEN) hostInstitution 2˙995˙640.00

Mappa


 Word cloud

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cryo    resolution    membrane    em    lipid    asymmetrical    fundamental    polytopic    molecular    co    structural    single    recycling    secyeg    protein    aring    ribosome    particles    visualize    function    proteins    translocon    integration    eukaryotic    structure    limited    complexes    particle   

 Obiettivo del progetto (Objective)

'Translation of the genetically encoded information into polypeptides, protein biosynthesis, is a central function executed by ribosomes in all cells. In the case of membrane protein synthesis, integration into the membrane usually occurs co-translationally and requires a ribosome-associated translocon (SecYEG/Sec61). This highly coordinated process is poorly understood, since high-resolution structural information is lacking. Although single particle cryo-electron microscopy (cryo-EM) has given invaluable structural insights for such dynamic ribosomal complexes, the resolution is so far limited to 5-10 Å for asymmetrical particles. Thus, the mechanistic depth and reliability of interpretation has accordingly been limited. Here, I propose to use single particle cryo-EM at improved, molecular resolution of 3-4 Å to study two fundamental ribosome-associated processes: (i) co-translational integration of polytopic membrane proteins and (ii) recycling of the eukaryotic ribosome. First, we will visualize nascent polytopic membrane proteins inserting into the lipid bilayer via the bacterial ribosome-bound SecYEG translocon. Notably, the translocon will be embedded in a lipid environment provided by so-called nanodiscs. Second, we will visualize in a similar approach membrane protein insertion via the YidC insertase, the main alternative translocon. Third, as a novel research direction, we will determine the structure and function of eukaryotic ribosome recycling complexes involving the ABC-ATPase RLI. The results will allow, together with functional biochemical data, an in-depth molecular structure-function analysis of these fundamental ribosome-associated processes. Moreover, reaching molecular resolution for asymmetrical particles by single particle cryo-EM will lift this technology to a level of analytical power approaching X-ray and NMR methods. ERC funding would allow for this highly challenging research to be conducted in an internationally competitive way in Europe.'

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