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Journal Article

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

MPS-Authors
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Paknia,  E.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Chari,  A.
Research Group of Structural Biochemistry and Mechanisms, MPI for Biophysical Chemistry, Max Planck Society;

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Stark,  H.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Fulltext (public)

2350875.pdf
(Publisher version), 3MB

Supplementary Material (public)

2350875_Suppl_1.pdf
(Supplementary material), 949KB

2350875_Suppl_2.pdf
(Supplementary material), 4MB

Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-82AD-3
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.