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SFSASP

Structural and Functional Studies of ATRX- Syndrome Protein

Total Cost €

0

EC-Contrib. €

0

Partnership

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 SFSASP project word cloud

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

malignancies    isothermal    alt    alternative    aging    small    structure    homeodomain    linked    phd    links    telomerase    genome    mental    independent    gene    harbours    electron    proteins    molecular    assays    pathologies    confers    packaged    energy    works    disease    severe    techniques    nmr    calorimetry    pericentromeric    alpha    identifies    remodellers    accessible    linking    consuming    rendered    cancer    family    maintenance    chromatin    interacting    blotting    accompanied    remodel    vivo    deposition    mechanism    unpacked    lack    plant    atr    functional    protein    ray    cryo    action    mutations    telomere    itself    atpase    cellular    western    angle    remodelling    enzymatic    helicase    interaction    scattering    crystallography    telomeres    shown    give    dna    regions    despite    daxx    syndrome    combination    domain    snf2    varied    atrx    constitutive    elucidate    eukaryotic    histone3    terminal    structural    localize    thalassemia    heterochromatin    interacts    retardation    lengthening    microscopy    complexes    functions    mounting    biophysical   

Project "SFSASP" data sheet

The following table provides information about the project.

Coordinator
THE UNIVERSITY OF SUSSEX 

Organization address
address: SUSSEX HOUSE FALMER
city: BRIGHTON
postcode: BN1 9RH
website: http://www.sussex.ac.uk

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 United Kingdom [UK]
 Project website http://www.sussex.ac.uk/lifesci/mancinilab/people
 Total cost 195˙454 €
 EC max contribution 195˙454 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2014
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2015
 Duration (year-month-day) from 2015-09-01   to  2017-08-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE UNIVERSITY OF SUSSEX UK (BRIGHTON) coordinator 195˙454.00

Map

 Project objective

The eukaryotic genome is packaged into chromatin, which needs to be unpacked to provide necessary access by cellular factors for varied cellular functions. However, DNA can be rendered accessible by the action of energy-consuming chromatin remodelling proteins. One such protein is ATRX that harbours an N-terminal plant homeodomain (PHD) and a C-terminal helicase domain that confers ATPase activity and identifies ATRX as a member of the snf2 family member of chromatin remodellers. ATRX has been shown to localize in vivo with constitutive heterochromatin in pericentromeric regions as well as telomeres where it works in complex with DAXX for the deposition of the Histone3.3. Mutations in the ATRX gene give rise to ATR-X syndrome, a severe X-linked mental retardation syndrome often accompanied by alpha-thalassemia. Mounting evidence links ATRX mutations to cancer and to malignancies that depend on a telomerase-independent pathway of telomere maintenance called the ‘alternative lengthening of telomeres (ALT) pathway, linking ATRX to aging. Despite these advances however, there is lack of understanding of the molecular mechanism of ATRX and of its role within these pathologies. The proposed research aims to investigate the structural and functional properties of ATRX, and to define at a molecular level how it interacts with DAXX to remodel chromatin. We will use a combination of biophysical techniques like NMR, Isothermal Calorimetry and western blotting to characterize ATRX interaction with partner proteins. X-ray crystallography, Cryo-electron microscopy and Small angle X-ray scattering techniques will be used to elucidate the structure of ATRX complexes. We will also design assays to measure the enzymatic activity of the ATRX snf2 domain by itself and in presence of DNA and/or its interacting partners. These studies will provide insight into a potential new mechanism of chromatin remodelling and will help us elucidate the consequences of disease-related ATRX mutations.

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

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