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Human Rpc5

RNA Polymerase III Rpc4/Rpc5 subcomplex and Selenocysteine tRNA transcription

Total Cost €

0

EC-Contrib. €

0

Partnership

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 Human Rpc5 project word cloud

Explore the words cloud of the Human Rpc5 project. It provides you a very rough idea of what is the project "Human Rpc5" about.

responsible    region    context    pol    similarity    similarly    crystallography    trnas    brf2    cellular    molecular    polymerase    homology    metazoans    terminus    lab    secys    yeast    homologue    eukaryotic    transcription    unpublished    trnasec    unanticipated    central    indicated    interacts    structure    dna    extension    isolation    exclusively    terminal    date    blockade    recruitment    characterise    secis    recruiting    trna    mechanism    prolonged    tbp    group    containing    preliminary    conserved    promoters    counterpart    proteins    dependent    interestingly    rnas    unravelled    link    phylogenetic    exception    small    protein    stress    size    oxidative    rna    translation    acting    mrnas    residues    regulatory    kingdom    determinants    participates    c37    accurate    eukaryotes    human    rpc5    suggests    prokaryotic    structural    subunit    relies    ray    govern    450    interaction    promoter    amongst    bound    recruits    predictions    evidences    selenocysteine    selb   

Project "Human Rpc5" data sheet

The following table provides information about the project.

Coordinator
THE INSTITUTE OF CANCER RESEARCH: ROYAL CANCER HOSPITAL 

Organization address
address: OLD BROMPTON ROAD 123
city: LONDON
postcode: SW7 3RP
website: www.icr.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.icr.ac.uk/our-research/research-divisions/division-of-structural-biology/vannini-group
 Total cost 183˙454 €
 EC max contribution 183˙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 2015-05-01   to  2017-04-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE INSTITUTE OF CANCER RESEARCH: ROYAL CANCER HOSPITAL UK (LONDON) coordinator 183˙454.00

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 Project objective

In higher eukaryotes, the RNA polymerase III (Pol III) participates in the transcription of small RNAs such as the tRNAs. RNA polymerase recruitment to their specific promoter relies on the activity of several transcription factors. Brf2 is a transcription factor that exclusively recruits RNA Pol III at the selenocysteine tRNA (tRNASec). Unpublished work from our group has unravelled an unanticipated central role of Brf2 in the oxidative stress response pathway, by acting as a cellular blockade during prolonged oxidative stress. We are interested in understanding the molecular determinants that govern RNA Pol III recruitment at tRNASec promoter and its interaction with Brf2-bound promoters. In general, RNA Pol III subunit’s size is conserved amongst the eukaryotic kingdom. However, an exception is the human Rpc5 subunit, whose C terminus has 450 residues that are not present in its yeast counterpart C37. Similarly to Brf2, the Rpc5 C-terminal extension is only present in higher metazoans, which suggests a phylogenetic link between these two proteins. The recruiting mechanism of RNA Pol III to Brf2-dependent promoters has not been described to date. Preliminary results in our lab provide evidences that indeed Rpc5 C terminus is responsible for the accurate recruitment of RNA Pol III at TBP/Brf2/DNA complex. Interestingly, structural homology predictions indicated that the human Rpc5 C-terminal extension is a eukaryotic homologue of the prokaryotic protein SelB, a factor that interacts with the tRNASec and with a specific region of mRNAs, the SECIS-element, during translation of SeCys containing proteins. This similarity suggests a regulatory role for Rpc5 C terminus in the interaction with the SECIS-element and/or the tRNASec. Our main objectives are to determine the structure of the Rpc5 C terminus in isolation and in complex with Brf2/TBP/DNA by X-ray crystallography and to characterise the role of Rpc5 C terminus in the context of tRNASec transcription.

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