Opendata, web and dolomites

RIBOFOLD SIGNED

Ribosome Processivity and Co-translational Protein Folding

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

 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.

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

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

Map

 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

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "RIBOFOLD" project.

For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.

Send me an  email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.

Thanks. And then put a link of this page into your project's website.

The information about "RIBOFOLD" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.1.)

PROGRESS (2019)

The Enemy of the Good: Towards a Theory of Moral Progress

Read More  

DISINTEGRATION (2019)

The Mass Politics of Disintegration

Read More  

NanoPD_P (2020)

High throughput multiplexed trace-analyte screening for diagnostics applications

Read More