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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.

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

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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