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Chap4Resp SIGNED

Catching in action a novel bacterial chaperone for respiratory complexes

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EC-Contrib. €

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 Chap4Resp project word cloud

Explore the words cloud of the Chap4Resp project. It provides you a very rough idea of what is the project "Chap4Resp" about.

mitochondria    solved    obtain    scrutinized    structure    macromolecular    biophysical    plasticity    quasiatomic    hydrolysis    clusters    realize    latest    fuelled    composition    diseases    fe    assembly    subunits    location    respiration    cofactors    cage    factories    subunit    45    membrane    provides    multidisciplinary    structural    stresses    resistant    cryoem    causing    requiring    investigation    maturation    genetic    mechanisms    coupling    microscopy    functional    optical    huge    cluster    spectroscopic    cryo    wire    correlative    life    imaging    ageing    situ    electron    cryogenic    chaperone    bacterial    transfer    conjunction    proteins    operates    snapshots    synergetic    homologue    gain    substrate    atp    interactions    pumping    minimal    protein    subtomogram    flow    14    cofactor    bacteria    context    data    metal    conserved    model    species    cytoplasm    coli    gradient    multisubunit    substrates    insertion    inner    flavin    proton    insights    combines    complexes    waste    reactive    power    energy    biogenesis    function    respiratory    interaction    cellular    techniques    oxygen    human    batteries    light    enigmatic    antibiotics    uncover    mechanism   

Project "Chap4Resp" data sheet

The following table provides information about the project.

Coordinator
CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE CNRS 

Organization address
address: RUE MICHEL ANGE 3
city: PARIS
postcode: 75794
website: www.cnrs.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]
 Project website http://www.ibs.fr/research/research-groups/methods-and-electron-microscopy-group/gutsche-team/
 Total cost 1˙999˙956 €
 EC max contribution 1˙999˙956 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2014-CoG
 Funding Scheme ERC-COG
 Starting year 2015
 Duration (year-month-day) from 2015-10-01   to  2021-09-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE CNRS FR (PARIS) coordinator 1˙999˙956.00

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 Project objective

Cellular respiration provides energy to power essential processes of life. Respiratory complexes are macromolecular batteries coupling electron flow through a wire of metal clusters and cofactors with proton transfer across the inner membrane of mitochondria and bacteria. Waste products of these cellular factories are reactive oxygen species causing ageing and diseases. Assembly and maturation mechanisms of respiratory complexes remain enigmatic because of their membrane location, multisubunit composition and cofactor insertion. E. coli Complex I, one of the largest membrane proteins, composed of 14 conserved subunits with 9 Fe/S clusters and a flavin, is a minimal model for its 45-subunit human homologue. When proton pumping by respiratory complexes is affected, bacteria become resistant to antibiotics requiring proton gradient for uptake. Based on the latest genetic data, we realize that the huge E. coli macromolecular cage, the structure of which we recently solved by cryo-electron microscopy (cryoEM), in conjunction with a novel protein cofactor, is a specific chaperone for Fe/S cluster biogenesis and assembly of respiratory complexes. This integrated multidisciplinary project combines cryoEM and other structural, biophysical and spectroscopic techniques, to uncover the functional mechanism of this emerging chaperone. The structural plasticity of the chaperone fuelled by ATP hydrolysis, and its interaction with Fe/S cluster biogenesis systems and the main respiratory complexes as a function of stresses, will be scrutinized to gain quasiatomic insights into the way the chaperone operates on its substrates. A novel technology for synergetic in situ investigation of protein complexes in the bacterial cytoplasm by optical imaging, state-of-the-art cryogenic correlative light and electron microscopy, and subtomogram analysis, will be developed and used to obtain snapshots of the chaperone-substrate interactions in the cellular context.

 Publications

year authors and title journal last update
List of publications.
2020 Alister Burt, C. Keith Cassidy, Peter Ames, Maria Bacia-Verloop, Megghane Baulard, Karine Huard, Zaida Luthey-Schulten, Ambroise Desfosses, Phillip J. Stansfeld, William Margolin, John S. Parkinson, Irina Gutsche
Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain
published pages: , ISSN: 2041-1723, DOI: 10.1038/s41467-020-14350-9
Nature Communications 11/1 2020-04-15
2019 Rosalba Lepore, Andriy Kryshtafovych, Markus Alahuhta, Harshul A. Veraszto, Yannick J. Bomble, Joshua C. Bufton, Alex N. Bullock, Cody Caba, Hongnan Cao, Owen R. Davies, Ambroise Desfosses, Matthew Dunne, Krzysztof Fidelis, Celia W. Goulding, Manickam Gurusaran, Irina Gutsche, Christopher J. Harding, Marcus D. Hartmann, Christopher S. Hayes, Andrzej Joachimiak, Petr G. Leiman, Peter Loppnau, Andre
Target highlights in CASP13: Experimental target structures through the eyes of their authors
published pages: 1037-1057, ISSN: 0887-3585, DOI: 10.1002/prot.25805
Proteins: Structure, Function, and Bioinformatics 87/12 2020-04-15
2019 Kandiah E, Carriel D, Garcia PS, Felix J, Banzhaf M, Kritikos G, Bacia-Verloop M, Brochier-Armanet C, Elsen S, Gutsche I.
Structure, Function, and Evolution of the Pseudomonas aeruginosa Lysine Decarboxylase LdcA
published pages: 1842-1854, ISSN: 0969-2126, DOI: 10.1016/j.str.2019.10.003
Structure Dec 3;27(12) 2020-04-15
2020 Matthew Jessop, Benoit Arragain, Roger Miras, Angélique Fraudeau, Karine Huard, Maria Bacia-Verloop, Patrice Catty, Jan Felix, Hélène Malet, Irina Gutsche
Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex
published pages: , ISSN: 2399-3642, DOI: 10.1038/s42003-020-0772-0
Communications Biology 3/1 2020-04-15
2019 Ambroise Desfosses, Hariprasad Venugopal, Tapan Joshi, Jan Felix, Matthew Jessop, Hyengseop Jeong, Jaekyung Hyun, J. Bernard Heymann, Mark R. H. Hurst, Irina Gutsche, Alok K. Mitra
Atomic structures of an entire contractile injection system in both the extended and contracted states
published pages: 1885-1894, ISSN: 2058-5276, DOI: 10.1038/s41564-019-0530-6
Nature Microbiology 4/11 2020-04-15
2019 Firas Khatib, Ambroise Desfosses, Brian Koepnick, Jeff Flatten, Zoran Popović, David Baker, Seth Cooper, Irina Gutsche, Scott Horowitz
Building de novo cryo-electron microscopy structures collaboratively with citizen scientists
published pages: e3000472, ISSN: 1545-7885, DOI: 10.1371/journal.pbio.3000472
PLOS Biology 17/11 2020-04-15
2019 Federica Laddomada, Mayara M. Miyachiro, Matthew Jessop, Delphine Patin, Viviana Job, Dominique Mengin-Lecreulx, Aline Le Roy, Christine Ebel, Cécile Breyton, Irina Gutsche, Andréa Dessen
The MurG glycosyltransferase provides an oligomeric scaffold for the cytoplasmic steps of peptidoglycan biosynthesis in the human pathogen Bordetella pertussis
published pages: , ISSN: 2045-2322, DOI: 10.1038/s41598-019-40966-z
Scientific Reports 9/1 2020-04-15
2019 Koen H. G. Verschueren, Clement Blanchet, Jan Felix, Ann Dansercoer, Dirk De Vos, Yehudi Bloch, Jozef Van Beeumen, Dmitri Svergun, Irina Gutsche, Savvas N. Savvides, Kenneth Verstraete
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle
published pages: 571-575, ISSN: 0028-0836, DOI: 10.1038/s41586-019-1095-5
Nature 568/7753 2020-04-15
2016 Eaazhisai Kandiah, Diego Carriel, Julien Perard, Hélène Malet, Maria Bacia, Kaiyin Liu, Sze W. S. Chan, Walid A. Houry, Sandrine Ollagnier de Choudens, Sylvie Elsen, Irina Gutsche
Structural insights into the Escherichia coli lysine decarboxylases andmolecular determinants of interaction with the AAA+ ATPase RavA
published pages: , ISSN: 2045-2322, DOI: 10.1038/srep24601
Scientific Reports 6/1 2019-10-14
2018 Diego Carriel, Pierre Simon Garcia, Florence Castelli, Patricia Lamourette, François Fenaille, Céline Brochier-Armanet, Sylvie Elsen, Irina Gutsche
A novel subfamily of bacterial AAT-fold basic amino acid decarboxylases and functional characterization of its first representative: Pseudomonas aeruginosa LdcA
published pages: , ISSN: 1759-6653, DOI: 10.1093/gbe/evy228
Genome Biology and Evolution 2019-10-14

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