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ItohRibo SIGNED

Structural study on mitochondrial ribosome assembly in human cells

Total Cost €

0

EC-Contrib. €

0

Partnership

0

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 ItohRibo project word cloud

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

combining    combination    abundant    ribosomal    ribosomes    nucleoids    resolution    mitoribosomal    cascade    sub    intermediates    nuclear    processed    lab    dynamics    fill    implicated    em    structural    formed    assembly    nascent    strength    proteins    microscopy    intricate    collaborators    cryo    lacking    tight    particle    maturation    human    electron    core    rna    stages    regulation    rrnas    proven    catalytic    compartments    insights    compartmentalized    encoded    gap    models    hundreds    tomography    transient    postulated    localize    heterogeneous    class    synthesizing    chain    et    cooperation    biochemical    relies    unknown    de    organelle    membrane    expand    mechanistic    13    harnessing    genome    mechanism    hierarchical    granules    complexes    molecules    mitochondria    completely    hydrophobic    characterization    mitoribosomes    transport    82    sections    milieus    editing    mitochondrion    reveal    populations    exclusively    expertise    scope    mature    cas9    mitoribosome    techniques    co    mt    rrna    specialized    mitochondrial    crispr    respiratory    single    complemented    novo    trans    assembled    folded    forming   

Project "ItohRibo" data sheet

The following table provides information about the project.

Coordinator
STOCKHOLMS UNIVERSITET 

Organization address
address: UNIVERSITETSVAGEN 10
city: STOCKHOLM
postcode: 10691
website: www.su.se

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 Sweden [SE]
 Total cost 173˙857 €
 EC max contribution 173˙857 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2017
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2018
 Duration (year-month-day) from 2018-06-21   to  2020-06-20

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    STOCKHOLMS UNIVERSITET SE (STOCKHOLM) coordinator 173˙857.00

Map

 Project objective

Human mitoribosome represents a distinct class of ribosomes that has specialized in synthesizing exclusively 13 hydrophobic membrane proteins, forming the catalytic core of the respiratory chain. The mature mitoribosome is composed of 82 nuclear encoded proteins and three mt-rRNAs. It is postulated that mitoribosomes are formed in an intricate and well-defined hierarchical process, involving hundreds of proteins and RNA molecules working in cooperation and under tight regulation. However, a structural insight into this process is completely lacking and most of the trans-factors remain unknown. I propose to fill this gap by harnessing CRISPR/Cas9 for genome editing in combination with the state of the art methods in single particle cryo-electron microscopy (cryo-EM). By combining these techniques with biochemical characterization, I will reveal mechanistic insights into how mitoribosomal proteins are assembled in a cascade while nascent mitochondrial rRNA molecules are processed and folded. Since high resolution cryo-EM allows now a unique ability to investigate heterogeneous ribosomal populations and built de novo models, the proposed work will not only reveal the maturation states, but also currently unknown factors implicated in the process. On the other hand, the mitochondrion is compartmentalized into sub-organelle sections such as nucleoids, RNA granules, and membrane-related milieus, and they co-localize with various stages of the mitoribosome assembly. I will also use cryo-electron tomography (cryo-ET) to expand the scope beyond the mitoribosomal complexes and reveal the dynamics of the maturation process and transport mechanism of the assembly intermediates between the sub-organelle compartments. Our approach relies on the most recently developed methodologies and proven strength of the lab complemented by specialized expertise of collaborators, aiming to characterize the transient and low abundant complexes in human mitochondria.

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

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