English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2.

Hamann, F., Schmitt, A., Favretto, F., Hofele, R., Neumann, P., Xiang, S. Q., et al. (2020). Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2. Proceedings of the National Academy of Sciences of the United States of America, 117(6), 2948-2956. doi:10.1073/pnas.1907960117.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0005-9324-C Version Permalink: http://hdl.handle.net/21.11116/0000-0005-B810-9
Genre: Journal Article

Files

show Files
hide Files
:
3190310.pdf (Publisher version), 2MB
Name:
3190310.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
3190310_Suppl.htm (Supplementary material), 201KB
Name:
3190310_Suppl.htm
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/xhtml+xml / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Hamann, F., Author
Schmitt, A., Author
Favretto, F., Author
Hofele, R.1, Author              
Neumann, P., Author
Xiang, S. Q.2, Author              
Urlaub, H.1, Author              
Zweckstetter, M.3, Author              
Ficner, R., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              
2Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              
3Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

Content

show
hide
Free keywords: DEAH-box ATPase; G-patch; Prp2; helicase; spliceosome
 Abstract: The spliceosome consists of five small RNAs and more than 100 proteins. Almost 50% of the human spliceosomal proteins were predicted to be intrinsically disordered or to contain disordered regions, among them the G-patch protein Spp2. The G-patch region of Spp2 binds to the DEAH-box ATPase Prp2, and both proteins together are essential for promoting the transition from the Bact to the catalytically active B* spliceosome. Here we show by circular dichroism and nuclear magnetic resonance (NMR) spectroscopy that Spp2 is intrinsically disordered in solution. Crystal structures of a complex consisting of Prp2-ADP and the G-patch domain of Spp2 demonstrate that the G-patch gains a defined fold when bound to Prp2. While the N-terminal region of the G-patch always folds into an α-helix in five different crystal structures, the C-terminal part is able to adopt two alternative conformations. NMR studies further revealed that the N-terminal part of the Spp2 G-patch, which is the most conserved region in different G-patch proteins, transiently samples helical conformations, possibly facilitating a conformational selection binding mechanism. The structural analysis unveils the role of conserved residues of the G-patch in the dynamic interaction mode of Spp2 with Prp2, which is vital to maintain the binding during the Prp2 domain movements needed for RNA translocation.

Details

show
hide
Language(s): eng - English
 Dates: 2020-01-232020-02-11
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1907960117
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 117 (6) Sequence Number: - Start / End Page: 2948 - 2956 Identifier: -