English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Cryo-EM structure of a human spliceosome activated for step 2 of splicing.

Bertram, K., Agafonov, D. E., Liu, W., Dybkov, O., Will, C. L., Hartmuth, K., et al. (2017). Cryo-EM structure of a human spliceosome activated for step 2 of splicing. Nature, 542(7641), 318-323. doi:10.1038/nature21079.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-93C2-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-93D9-B
Genre: Journal Article

Files

show Files
hide Files
:
2404509.pdf (Publisher version), 17MB
 
File Permalink:
-
Name:
2404509.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), Göttingen; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2404509_Suppl_1.html (Supplementary material), 98KB
Name:
2404509_Suppl_1.html
Description:
-
Visibility:
Public
MIME-Type / Checksum:
text/html / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2404509_Suppl_2.pdf (Supplementary material), 2MB
Name:
2404509_Suppl_2.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Bertram, K.1, Author              
Agafonov, D. E.2, Author              
Liu, W.1, Author              
Dybkov, O.2, Author              
Will, C. L.2, Author              
Hartmuth, K.2, Author              
Urlaub, H.3, Author              
Kastner, B.2, Author              
Stark, H.1, Author              
Lührmann, R.2, Author              
Affiliations:
1Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              
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: -
 Abstract: Spliceosome rearrangements facilitated by RNA helicase PRP16 before catalytic step two of splicing are poorly understood. Here we report a 3D cryo-electron microscopy structure of the human spliceosomal C complex stalled directly after PRP16 action (C*). The architecture of the catalytic U2–U6 ribonucleoprotein (RNP) core of the human C* spliceosome is very similar to that of the yeast pre-Prp16 C complex. However, in C* the branched intron region is separated from the catalytic centre by approximately 20 Å, and its position close to the U6 small nuclear RNA ACAGA box is stabilized by interactions with the PRP8 RNase H-like and PRP17 WD40 domains. RNA helicase PRP22 is located about 100 Å from the catalytic centre, suggesting that it destabilizes the spliced mRNA after step two from a distance. Comparison of the structure of the yeast C and human C* complexes reveals numerous RNP rearrangements that are likely to be facilitated by PRP16, including a large-scale movement of the U2 small nuclear RNP.

Details

show
hide
Language(s): eng - English
 Dates: 2017-01-112017-02-16
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Internal
 Identifiers: DOI: 10.1038/nature21079
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 542 (7641) Sequence Number: - Start / End Page: 318 - 323 Identifier: -