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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.

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

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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