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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.

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

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

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 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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