English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  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.

Item is

Files

show Files
hide Files
:
2566555.pdf (Publisher version), 6MB
 
File Permalink:
-
Name:
2566555.pdf
Description:
-
OA-Status:
Visibility:
Restricted ( Max Planck Society (every institute); )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 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              

Content

show
hide
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.

Details

show
hide
Language(s): eng - English
 Dates: 2018-03-152018-03-15
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.molcel.2018.02.022
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Molecular Cell
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 69 (6) Sequence Number: - Start / End Page: 979 - 992 Identifier: -