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TransFold SIGNED

Molecular Biology of Nascent Chains: Co-translational folding and assembly of proteins in eukaryotes

Total Cost €

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EC-Contrib. €

0

Partnership

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 TransFold project word cloud

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

profiles    sequence    rarity    chains    biology    identification    complemented    differences    prevalence    subunit    chaperone    expose    paradigm    ribosome    assembly    folding    synthesized    eukaryotes    drives    unexplored    resolution    molecular    interaction    variations    regulatory    initiates    constellations    powerful    complexes    diffusing    co    differing    dependent    intersection    collision    biological    translation    profiling    gene    breaking    largely    mrnas    conceptually    suggests    unravel    speed    protein    critical    shift    natively    timing    operons    influencing    coding    residue    ribosomes    local    bacteria    membrane    guide    fundamental    localized    establishing    random    translational    folded    encoding    specifies    linked    imply    underpinning    posttranslational    integration    chain    basic    serp    occurs    subunits    interactions    final    enzyme    assisted    oligomeric    efficiency    cells    proteins    act    dynamic    biochemistry    selective    nascent    near    translationally    synthesis    machineries    yeast    impacts    chaperones    organization    ground    interplay    localization    mrna    definition    supporting    hubs    depends    microscopy   

Project "TransFold" data sheet

The following table provides information about the project.

Coordinator
RUPRECHT-KARLS-UNIVERSITAET HEIDELBERG 

Organization address
address: SEMINARSTRASSE 2
city: HEIDELBERG
postcode: 69117
website: www.uni-heidelberg.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˙069˙000 €
 EC max contribution 2˙069˙000 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2016-ADG
 Funding Scheme ERC-ADG
 Starting year 2017
 Duration (year-month-day) from 2017-10-01   to  2022-09-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    RUPRECHT-KARLS-UNIVERSITAET HEIDELBERG DE (HEIDELBERG) coordinator 2˙069˙000.00

Map

 Project objective

Biological activity of cells depends on timely production of natively folded proteins by powerful translation and folding machineries. At a critical regulatory intersection of translation and folding, ribosomes act as integration hubs coordinating chaperone, enzyme and membrane targeting factor activity, and mRNA coding sequence specifies local changes in translation speed, influencing folding. Final assembly of proteins into oligomeric complexes however, has long been considered posttranslational and dependent on random collision of fully synthesized diffusing subunits. In a shift of paradigm our recent evidence now suggests that in bacteria, assembly initiates co-translationally assisted by chaperones, and gene organization into operons drives co-localized translation of complex subunits that impacts efficiency of assembly. Fundamental differences in eukaryotes such as rarity of operons and differing chaperone constellations imply a widely different folding and assembly biology, which remains largely unexplored. Our development of the selective ribosome profiling (SeRP) method now allows ground-breaking identification and definition of dynamic interactions of nascent chains, at near-residue resolution. Using SeRP with supporting biochemistry and microscopy, we will unravel the nascent chain molecular biology underpinning protein folding and assembly in yeast. Specifically, we will establish (1) basic features and prevalence of co-translational protein assembly, (2) how chaperones guide co-translational protein folding to affect assembly, (3) whether translation of subunit-encoding mRNAs is spatially organized, and if so, how this occurs, and (4) to what extent translation speed variations affect assembly. Subunit interaction profiles complemented by mRNA localization will expose the timing and interplay of protein folding and assembly steps linked to protein synthesis, establishing a detailed conceptually new biology of complex assembly in eukaryotes.

 Publications

year authors and title journal last update
List of publications.
2019 Günter Kramer, Ayala Shiber, Bernd Bukau
Mechanisms of Cotranslational Maturation of Newly Synthesized Proteins
published pages: 337-364, ISSN: 0066-4154, DOI: 10.1146/annurev-biochem-013118-111717
Annual Review of Biochemistry 88/1 2019-08-29

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