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ItohRibo SIGNED

Structural study on mitochondrial ribosome assembly in human cells

Total Cost €

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

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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