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TransFold SIGNED

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

Total Cost €


EC-Contrib. €






 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.

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

Project "TransFold" data sheet

The following table provides information about the project.


Organization address
postcode: 69117

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


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 


 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.


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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