title: Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.
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.
authors.affiliation: LOEWE Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Philipps-University Marburg, Hans-Meerwein-Straße, Marburg D-35043, Germany.
authors.forename: Patrick
authors.initials: P
authors.lastname: Pausch
authors.affiliation: Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, Fribourg CH-1700, Switzerland.
authors.forename: Ujjwala
authors.initials: U
authors.lastname: Singh
authors.affiliation: Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg D-61920, Germany.
authors.forename: Yasar Luqman
authors.identifier: 0000000243641372
authors.initials: YL
authors.lastname: Ahmed
authors.affiliation: Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, Fribourg CH-1700, Switzerland.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Pillet
authors.affiliation: Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, Fribourg CH-1700, Switzerland.
authors.forename: Guillaume
authors.initials: G
authors.lastname: Murat
authors.affiliation: LOEWE Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Philipps-University Marburg, Hans-Meerwein-Straße, Marburg D-35043, Germany.
authors.forename: Florian
authors.initials: F
authors.lastname: Altegoer
authors.affiliation: Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg D-61920, Germany.
authors.forename: Gunter
authors.initials: G
authors.lastname: Stier
authors.affiliation: Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg D-61920, Germany.
authors.forename: Matthias
authors.initials: M
authors.lastname: Thoms
authors.affiliation: Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg D-61920, Germany.
authors.forename: Ed
authors.initials: E
authors.lastname: Hurt
authors.affiliation: Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg D-61920, Germany.
authors.forename: Irmgard
authors.initials: I
authors.lastname: Sinning
authors.affiliation: LOEWE Center for Synthetic Microbiology (SYNMIKRO) and Department of Chemistry, Philipps-University Marburg, Hans-Meerwein-Straße, Marburg D-35043, Germany.
authors.forename: Gert
authors.initials: G
authors.lastname: Bange
authors.affiliation: Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, Fribourg CH-1700, Switzerland.
authors.forename: Dieter
authors.initials: D
authors.lastname: Kressler
mesh_terms: D002597:Chaetomium / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal / Q000502:physiology; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
chemical_list: D005656:Fungal Proteins; D018832:Molecular Chaperones; D012269:Ribosomal Proteins