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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.

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

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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