Proteomics

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Early Scanning of Nascent Polypeptides inside the Ribosomal Tunnel by NAC

ABSTRACT: In this study, NAC was UV-crosslinked using the photo-crosslinking amino acid p-benzoyl-L-phenylalanine (pBPA) in order to determine specific interaction sites of the alphaNAC N-terminus in the native protein structure. Furthermore, quantitative chemical crosslinking coupled to mass spectrometry (q-XL-MS) was used to compare crosslink abundances of a NAC mutant versus wild type NAC in order to determine the influence of the mutated motive on the structural dynamics of NAC.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human) Caenorhabditis Elegans

SUBMITTER: Florian Stengel  

LAB HEAD: Florian Stengel

PROVIDER: PXD011995 | Pride | 2019-07-25

REPOSITORIES: Pride

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F1811_sailerc_005_006_band_1_plus_UV_Interlink_merged.mgf Mgf
F1811_sailerc_005_band_1_plus_UV_Interlink.raw Raw
F1811_sailerc_006_band_1_plus_UV_Interlink.raw Raw
F1811_sailerc_013_014_band_3_plus_UV_Intralink_merged.mgf Mgf
F1811_sailerc_013_band_3_plus_UV_alphaNAC_Intralink.raw Raw
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Publications

Cotranslational processing of newly synthesized proteins is fundamental for correct protein maturation. Protein biogenesis factors are thought to bind nascent polypeptides not before they exit the ribosomal tunnel. Here, we identify a nascent chain recognition mechanism deep inside the ribosomal tunnel by an essential eukaryotic cytosolic chaperone. The nascent polypeptide-associated complex (NAC) inserts the N-terminal tail of its β subunit (N-βNAC) into the ribosomal tunnel to sense substrates  ...[more]

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