Proteomics

Dataset Information

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N-terminal acetylation of yeast NAT-A mutants

ABSTRACT: Protein-protein interactions are fundamental to all cellular activities, with the ribosome increasingly recognized as a central platform steering the dynamics of nascent-chain interactions. In our focus on conserved N-terminal acetyltransferases (NATs), we identified distinct co-translational assembly pathways. This distinction persisted even among highly homologous subunits, with some playing contrasting roles. Notably, we found that only a few residues act as “hotspots”, initiating co-translational assembly interactions as they emerge from the ribosome exit tunnel. The significance of these hotspots was further validated in vivo through N-terminomics studies.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Oded Kleifeld  

LAB HEAD: Ayala Shiber

PROVIDER: PXD048082 | Pride | 2024-06-22

REPOSITORIES: Pride

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2023-04-27-decoys-reviewed-isoforms-contam-UP000002311.fas Other
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Seq76231_QE3.mzML Mzml
Seq76231_QE3.pep.xml Pepxml
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Publications

Diverging co-translational protein complex assembly pathways are governed by interface energy distribution.

Venezian Johannes J   Bar-Yosef Hagit H   Ben-Arie Zilberman Hila H   Cohen Noam N   Kleifeld Oded O   Fernandez-Recio Juan J   Glaser Fabian F   Shiber Ayala A  

Nature communications 20240325 1

Protein-protein interactions are at the heart of all cellular processes, with the ribosome emerging as a platform, orchestrating the nascent-chain interplay dynamics. Here, to study the characteristics governing co-translational protein folding and complex assembly, we combine selective ribosome profiling, imaging, and N-terminomics with all-atoms molecular dynamics. Focusing on conserved N-terminal acetyltransferases (NATs), we uncover diverging co-translational assembly pathways, where highly  ...[more]

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