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DynamicAssemblies SIGNED

Conformational studies of highly dynamic viral replication complexes

Total Cost €

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EC-Contrib. €

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Partnership

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 DynamicAssemblies project word cloud

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

structure    cycle    tools    basis    negative    measles    complexes    cellular    describe    solution    chaperoning    genomes    viral    resolved    nmr    nucleoprotein    replication    understand    pathogens    paramyxoviruses    initiating    kinetics    descriptions    assembly    conformational    regulatory    extensive    spectroscopy    exploited    enigmatic    unexplained    elaboration    interaction    liquid    disorder    observation    form    dynamics    nucleocapsids    requiring    synthesized    simulation    machinery    interactions    inaccessible    genetic    host    revolutionizing    droplets    fluorescence    organelles    intrinsic    newly    translational    proteins    strand    mechanisms    parsimoniously    previously    sites    flexibility    unfolded    extremely    trajectories    soluble    human    crystallography    biology    engineering    functional    resolution    chemical    membraneless    post    saxs    molecular    time    disordered    rna    assemble    cryoem    exhibit    ncs    atomic    phosphoprotein    physical    regions    transcription    tetrameric    viruses    poorly    intrinsically    combined    rendered    normally    express    modification    mixed    ongoing    dangerous   

Project "DynamicAssemblies" data sheet

The following table provides information about the project.

Coordinator
COMMISSARIAT A L ENERGIE ATOMIQUE ET AUX ENERGIES ALTERNATIVES 

Organization address
address: RUE LEBLANC 25
city: PARIS 15
postcode: 75015
website: www.cea.fr

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 France [FR]
 Total cost 2˙499˙150 €
 EC max contribution 2˙499˙150 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2018-ADG
 Funding Scheme ERC-ADG
 Starting year 2019
 Duration (year-month-day) from 2019-11-01   to  2024-10-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    COMMISSARIAT A L ENERGIE ATOMIQUE ET AUX ENERGIES ALTERNATIVES FR (PARIS 15) coordinator 2˙499˙150.00

Map

 Project objective

Paramyxoviruses, including, measles and a number of dangerous human pathogens, are negative strand RNA viruses that express their own machinery for transcription and replication. Different interactions between the nucleoprotein (N) and the phosphoprotein (P) are essential for chaperoning and assembly of N on newly synthesized RNA genomes to form nucleocapsids (NCs), as well as for initiating replication and transcription. Both N and tetrameric P exhibit extensive conformational disorder, with very long, unfolded regions that host important post-translational modification sites as well as regulatory interactions with host and viral partners. The presence of this level of disorder, in viruses whose genetic information is normally so parsimoniously exploited, remains unexplained. The elaboration of time-resolved, atomic resolution descriptions of the interaction trajectories of these highly disordered N:P complexes is extremely challenging, requiring the development of adapted methodologies that can account for their intrinsic flexibility. The role of N and P has been rendered yet more enigmatic following our recent observation that when mixed in solution they form liquid-like droplets. Such membraneless organelles are revolutionizing our understanding of cellular chemical biology, although their physical basis is poorly understood. Our aim is to describe these important complexes at atomic resolution, in particular to understand the role of the extensive conformational dynamics of N and P in the replication cycle. Our recent success in engineering soluble N:P complexes from measles that assemble into NCs, combined with ongoing development of NMR-based methods to investigate the structure, dynamics and interaction kinetics of large, intrinsically disordered proteins, fluorescence spectroscopy, cryoEM, SAXS, crystallography and molecular simulation, will provide the essential tools to investigate the functional mechanisms of these previously inaccessible complexes.

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

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