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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.

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

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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