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  Prp19/Pso4 is an autoinhibited ubiquitin ligase activated by stepwise assembly of three splicing factors.

Rocha de Moura, T., Mozaffari-Jovin, S., Szabo, C. Z. K., Schmitzova, J., Dybkov, O., Cretu, C., et al. (2018). Prp19/Pso4 is an autoinhibited ubiquitin ligase activated by stepwise assembly of three splicing factors. Molecular Cell, 69(6), 979-992. doi:10.1016/j.molcel.2018.02.022.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-F722-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-B05A-1
Genre: Journal Article

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 Creators:
Rocha de Moura, T.1, Author              
Mozaffari-Jovin, S.2, Author              
Szabo, C. Z. K., Author
Schmitzova, J.1, Author              
Dybkov, O.2, Author              
Cretu, C.1, Author              
Kachala, M., Author
Svergun, D., Author
Urlaub, H.3, Author              
Lührmann, R.2, Author              
Pena, V.1, Author              
Affiliations:
1Research Group of Macromolecular Crystallography, MPI for Biophysical Chemistry, Max Planck Society, ou_2035293              
2Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              
3Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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Free keywords: Prp19/NTC complex; DNA damage response; pre-mRNA splicing; E3 ubiquitin ligase
 Abstract: Human nineteen complex (NTC) acts as a multimeric E3 ubiquitin ligase in DNA repair and splicing. The transfer of ubiquitin is mediated by Prp19-a homotetrameric component of NTC whose elongated coiled coils serve as an assembly axis for two other proteins called SPF27 and CDC5L. We find that Prp19 is inactive on its own and have elucidated the structural basis of its autoinhibition by crystallography and mutational analysis. Formation of the NTC core by stepwise assembly of SPF27, CDC5L, and PLRG1 onto the Prp19 tetramer enables ubiquitin ligation. Protein-protein crosslinking of NTC, functional assays in vitro, and assessment of its role in DNA damage response provide mechanistic insight into the organization of the NTC core and the communication between PLRG1 and Prp19 that enables E3 activity. This reveals a unique mode of regulation for a complex E3 ligase and advances understanding of its dynamics in various cellular pathways.

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Language(s): eng - English
 Dates: 2018-03-152018-03-15
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2018.02.022
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 69 (6) Sequence Number: - Start / End Page: 979 - 992 Identifier: -