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DECOR SIGNED

Dynamic assembly and exchange of RNA polymerase II CTD factors

Total Cost €

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EC-Contrib. €

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Partnership

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Project "DECOR" data sheet

The following table provides information about the project.

Coordinator
Masarykova univerzita 

Organization address
address: Zerotinovo namesti 9
city: BRNO STRED
postcode: 60177
website: http://www.muni.cz

contact info
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name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Czech Republic [CZ]
 Project website https://www.ceitec.eu/decor-dynamic-assembly-and-exchange-of-rna-polymerase-ii-ctd-factors/t2960
 Total cost 1˙844˙603 €
 EC max contribution 1˙844˙603 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2014-CoG
 Funding Scheme ERC-COG
 Starting year 2015
 Duration (year-month-day) from 2015-08-01   to  2020-07-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    Masarykova univerzita CZ (BRNO STRED) coordinator 1˙844˙603.00

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 Project objective

The C-terminal domain (CTD) of the RNA polymerase II (RNAPII) largest subunit coordinates co-transcriptional processing and it is decorated by many processing factors throughout the transcription cycle. The composition of this supramolecular assembly is diverse and highly dynamic. Many of the factors associate with RNAPII weakly and transiently, and the association is dictated by different post-translational modification patterns and conformational changes of the CTD. To determine how these accessory factors assemble and exchange on the CTD of RNAPII has remained a major challenge. Here, we aim to unravel the structural and mechanistic bases for the dynamic assembly of RNAPII CTD with its processing factors. Using NMR, we will determine high-resolution structures of several protein factors bound to the CTD carrying specific modifications. This will enable to decode how CTD modification patterns stimulate or prevent binding of a given processing factor. We will also establish the structural and mechanistic bases of proline isomerisation in the CTD that control the timing of isomer-specific protein-protein interactions. Next, we will combine NMR and SAXS approaches to unravel how the overall CTD structure is remodelled by binding of multiple copies of processing factors and how these factors cross-talk with each other. Finally, we will elucidate a mechanistic basis for the exchange of processing factors on the CTD. Our study will answer the long-standing questions of how the overall CTD structure is modulated on binding to processing factors, and whether these factors cross-talk and compete with each other. The level of detail that we aim to achieve is currently not available for any transient molecular assemblies of such complexity. In this respect, the project will also provide knowledge and methodology for further studies of large and highly flexible molecular assemblies that still remain poorly understood.

 Publications

year authors and title journal last update
List of publications.
2020 Zhong Han, Olga Jasnovidova, Nouhou Haidara, Agnieszka Tudek, Karel Kubicek, Domenico Libri, Richard Stefl, Odil Porrua
Termination of non‐coding transcription in yeast relies on both an RNA Pol II CTD interaction domain and a CTD‐mimicking region in Sen1
published pages: , ISSN: 0261-4189, DOI: 10.15252/embj.2019101548
The EMBO Journal 39/7 2020-04-15
2019 Pavel Brázda, Ondrej Šedo, Karel Kubíček, Richard Štefl
Efficient and robust preparation of tyrosine phosphorylated intrinsically disordered proteins
published pages: 16-22, ISSN: 0736-6205, DOI: 10.2144/btn-2019-0033
BioTechniques 67/1 2020-04-01
2017 Olga Jasnovidova, Tomas Klumpler, Karel Kubicek, Sergei Kalynych, Pavel Plevka, Richard Stefl
Structure and dynamics of the RNAPII CTDsome with Rtt103
published pages: 11133-11138, ISSN: 0027-8424, DOI: 10.1073/pnas.1712450114
Proceedings of the National Academy of Sciences 114/42 2019-06-07
2017 Olga Jasnovidova, Magdalena Krejcikova, Karel Kubicek, Richard Stefl
Structural insight into recognition of phosphorylated threonine‐4 of RNA polymerase II C‐terminal domain by Rtt103p
published pages: 906-913, ISSN: 1469-221X, DOI: 10.15252/embr.201643723
EMBO reports 18/6 2019-06-07

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