English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The ribosome cooperates with the assembly chaperone pICln to initiate formation of snRNPs.

Paknia, E., Chari, A., Stark, H., & Fischer, U. (2016). The ribosome cooperates with the assembly chaperone pICln to initiate formation of snRNPs. Cell Reports, 16(12), 3103-3112. doi:10.1016/j.celrep.2016.08.047.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-82AD-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-0989-D
Genre: Journal Article

Files

show Files
hide Files
:
2350875.pdf (Publisher version), 3MB
Name:
2350875.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
:
2350875_Suppl_1.pdf (Supplementary material), 949KB
Name:
2350875_Suppl_1.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2350875_Suppl_2.pdf (Supplementary material), 4MB
Name:
2350875_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:
Paknia, E.1, Author              
Chari, A.1, Author              
Stark, H.1, Author              
Fischer, U., Author
Affiliations:
1Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              

Content

show
hide
Free keywords: assembly chaperone; pICln; ribosome; snRNPs
 Abstract: The formation of macromolecular complexes within the crowded environment of cells often requires aid from assembly chaperones. PRMT5 and SMN complexes mediate this task for the assembly of the common core of pre-mRNA processing small nuclear ribonucleoprotein particles (snRNPs). Core formation is initiated by the PRMT5-complex subunit pICln, which pre-arranges the core proteins into spatial positions occupied in the assembled snRNP. The SMN complex then accepts these pICln-bound proteins and unites them with small nuclear RNA (snRNA). Here, we have analyzed how newly synthesized snRNP proteins are channeled into the assembly pathway to evade mis-assembly. We show that they initially remain bound to the ribosome near the polypeptide exit tunnel and dissociate upon association with pICln. Coincident with its release activity, pICln ensures the formation of cognate heterooligomers and their chaperoned guidance into the assembly pathway. Our study identifies the ribosomal quality control hub as a site where chaperone-mediated assembly of macromolecular complexes can be initiated.

Details

show
hide
Language(s): eng - English
 Dates: 2016-09-20
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.celrep.2016.08.047
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Cell Reports
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 16 (12) Sequence Number: - Start / End Page: 3103 - 3112 Identifier: -