Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones

Patrick Pausch, Ujjwala Singh, Yasar Luqman Ahmed, Benjamin Pillet, Guillaume Murat, Florian Altegoer, Gunter Stier, Matthias Thoms, Ed Hurt, Irmgard Sinning, Gert Bange () and Dieter Kressler ()
Additional contact information
Patrick Pausch: Philipps-University Marburg
Ujjwala Singh: Unit of Biochemistry, University of Fribourg
Yasar Luqman Ahmed: Heidelberg University Biochemistry Center (BZH)
Benjamin Pillet: Unit of Biochemistry, University of Fribourg
Guillaume Murat: Unit of Biochemistry, University of Fribourg
Florian Altegoer: Philipps-University Marburg
Gunter Stier: Heidelberg University Biochemistry Center (BZH)
Matthias Thoms: Heidelberg University Biochemistry Center (BZH)
Ed Hurt: Heidelberg University Biochemistry Center (BZH)
Irmgard Sinning: Heidelberg University Biochemistry Center (BZH)
Gert Bange: Philipps-University Marburg
Dieter Kressler: Unit of Biochemistry, University of Fribourg

Nature Communications, 2015, vol. 6, issue 1, 1-15

Abstract: Abstract Exponentially growing yeast cells produce every minute >160,000 ribosomal proteins. Owing to their difficult physicochemical properties, the synthesis of assembly-competent ribosomal proteins represents a major challenge. Recent evidence highlights that dedicated chaperone proteins recognize the N-terminal regions of ribosomal proteins and promote their soluble expression and delivery to the assembly site. Here we explore the intuitive possibility that ribosomal proteins are captured by dedicated chaperones in a co-translational manner. Affinity purification of four chaperones (Rrb1, Syo1, Sqt1 and Yar1) selectively enriched the mRNAs encoding their specific ribosomal protein clients (Rpl3, Rpl5, Rpl10 and Rps3). X-ray crystallography reveals how the N-terminal, rRNA-binding residues of Rpl10 are shielded by Sqt1’s WD-repeat β-propeller, providing mechanistic insight into the incorporation of Rpl10 into pre-60S subunits. Co-translational capturing of nascent ribosomal proteins by dedicated chaperones constitutes an elegant mechanism to prevent unspecific interactions and aggregation of ribosomal proteins on their road to incorporation.

Date: 2015
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms8494 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8494

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms8494

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().