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SpliceosomeStructure

Structural role of protein splicing factors in promoting an active configuration of the spliceosome's RNA catalytic core

Total Cost €

0

EC-Contrib. €

0

Partnership

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 SpliceosomeStructure project word cloud

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

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Project "SpliceosomeStructure" data sheet

The following table provides information about the project.

Coordinator
UNITED KINGDOM RESEARCH AND INNOVATION 

There are not information about this coordinator. Please contact Fabio for more information, thanks.

 Coordinator Country United Kingdom [UK]
 Project website https://www2.mrc-lmb.cam.ac.uk/groups/nagai/structure-gallery/
 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 2016
 Duration (year-month-day) from 2016-03-01   to  2018-02-28

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNITED KINGDOM RESEARCH AND INNOVATION UK (SWINDON) coordinator 183˙454.00
2    MEDICAL RESEARCH COUNCIL UK (SWINDON) coordinator 0.00

Map

 Project objective

The spliceosome is a ribonucleoprotein machine that excises introns from pre-messenger RNAs. During my phD, I identified RNA ligands for the magnesium ions that catalyze these splicing reactions and showed that the spliceosomal U6 and U2 small nuclear RNAs form a structure resembling group II self-splicing intron RNAs. Although the spliceosome's catalytic core is RNA-based, numerous spliceosomal proteins promote the proper catalytic fold of this RNA core, juxtapose the reactive pre-mRNA elements with the U6 metal sites, and regulate spliceosome dynamics during the splicing cycle. Indeed, the Prp8 protein cross-links with the critical nucleotides of the catalytic RNA core and its crystal structure, reported recently by the host laboratory, revealed a cavity that accommodates the catalytic RNA core. Moreover, several helicases, such as Brr2 and Prp16, promote an active configuration of the U2/U6 RNA core and associated proteins and regulate their dynamics. The arrangement of such proteins in the assembled spliceosome and their interactions with the RNA core is presently unknown due to the lack of high-resolution structures of any spliceosomal complexes. I will study biochemically in vitro the interactions between the U2/U6 core and key proteins necessary for an active fold of the RNA core, with the goal of reconstituting and solving the high-resolution structure of a minimal active U2/U6 RNA core in complex with the reactive pre-mRNA sites and surrounding proteins including Prp8. In parallel, I will employ recent advances in cryo-electron microscopy sample preparation, imaging, and data processing, which were pioneered at the host institute, to obtain high-resolution (at least 7 Angstroms) three-dimensional reconstructions of endogenous fully assembled spliceosomes stalled at specific splicing stages. These studies promise to provide unprecedented structural insihgt into the configuration and dynamics of key RNA and protein elements of the spliceosome.

 Publications

year authors and title journal last update
List of publications.
2017 Max E. Wilkinson, Sebastian M. Fica, Wojciech P. Galej, Christine M. Norman, Andrew J. Newman, Kiyoshi Nagai
Postcatalytic spliceosome structure reveals mechanism of 3′–splice site selection
published pages: 1283-1288, ISSN: 0036-8075, DOI: 10.1126/science.aar3729
Science 358/6368 2019-06-13

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

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