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Structural study on mitochondrial ribosome assembly in human cells

Total Cost €


EC-Contrib. €






 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.

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

Project "ItohRibo" data sheet

The following table provides information about the project.


Organization address
postcode: 10691

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


Take a look of project's partnership.

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


 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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