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RIBOFOLD SIGNED

Ribosome Processivity and Co-translational Protein Folding

Total Cost €

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EC-Contrib. €

0

Partnership

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 RIBOFOLD project word cloud

Explore the words cloud of the RIBOFOLD project. It provides you a very rough idea of what is the project "RIBOFOLD" about.

protein    translationally    resolved    temporal    folding    molecular    human    bound    pauses    peptide    resolution    assays    chaperone    particle    processivity    auxiliary    quality    co    pausing    vitro    domain    vivo    science    electron    domains    ribosomal    stalled    microscopy    recognition    horizons    exit    causes    translation    understand    link    start    defects    trigger    events    cryo    transient    nascent    starts    probe    molecule    space    fold    conformational    data    polypeptide    analyze    monitoring    translational    ribosome    mathematical    solved    structures    modulated    setups    tunnel    complexes    al    diseases    structure    synthesized    speed    ensemble    mechanisms    landscape    buhr    2016    first    intermediates    biogenesis    holtkamp    confined    time    proteins    poorly    cell    follow    modeling    mol    2015    signal    basis    types    single    kinetics    simultaneously    trajectories    profiling    proof    et   

Project "RIBOFOLD" data sheet

The following table provides information about the project.

Coordinator
MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV 

Organization address
address: HOFGARTENSTRASSE 8
city: Munich
postcode: 80539
website: www.mpg.de

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Germany [DE]
 Total cost 2˙482˙600 €
 EC max contribution 2˙482˙600 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2017-ADG
 Funding Scheme ERC-ADG
 Starting year 2018
 Duration (year-month-day) from 2018-08-01   to  2023-07-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV DE (Munich) coordinator 2˙482˙600.00

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 Project objective

Protein domains start to fold co-translationally while they are being synthesized on the ribosome. Co-translational folding starts in the confined space of the ribosomal polypeptide exit tunnel and is modulated by the speed of translation. Although defects in protein folding cause many human diseases, the mechanisms of co-translational folding and the link between the speed of translation and the quality of protein folding is poorly understood. Here I propose to study when, where and how proteins emerging from the ribosome start to fold, how the ribosome and auxiliary proteins bound at the polypeptide exit affect nascent peptide folding, what causes ribosome pausing during translation, and how pausing affects nascent peptide folding. Our recent results (Holtkamp et al., Science 2015; Buhr et al., Mol Cell 2016) provide the proof of principle for monitoring translation and protein folding simultaneously at high temporal resolution. First, we will follow translation processivity and folding trajectories for proteins of different domain structure types using time-resolved ensemble kinetics and single-molecule setups. The structures of complexes with stalled folding intermediates will be solved by cryo-electron microscopy. Second, we will investigate the effects of the chaperone trigger factor, the signal recognition particle, and other protein biogenesis factors on the folding landscape. Third, we will analyze transient ribosome pauses in vivo (based on ribosome profiling data) and in vitro (based on time-resolved translation assays and mathematical modeling) and identify the events that cause pausing. Finally, we will probe how changes in translational processivity affect the conformational landscape of a protein. We expect that these results will open new horizons in understanding co-translational protein folding and will help to understand the molecular basis of many diseases.

 Publications

year authors and title journal last update
List of publications.
2020 Marija Liutkute, Ekaterina Samatova, Marina V. Rodnina
Cotranslational Folding of Proteins on the Ribosome
published pages: 97, ISSN: 2218-273X, DOI: 10.3390/biom10010097
Biomolecules 10/1 2020-02-13

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