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Proteome-wide analysis of elongating nascent polypeptide chains - mouse primary neuron DIV5 vs DIV14

ABSTRACT: Cellular global translation is often measured using ribosome profiling or quantitative mass spectrometry, but these methods do not provide direct information at the level of elongating nascent polypeptide chains (NPCs) and associated co-translational events. We combine quantitative proteomics, pulse labeling with puromycin, and stable isotope-labeled amino acids to analyze thousands of NPCs. Our approach enables global analyses of translational responses and co-translational modifications, providing a framework for dissecting co-translational regulations proteome-wide. NPCs from mouse primary neurons were analyzed in triplicates.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Yasushi Ishihama

PROVIDER: PXD026346 | JPOST Repository | Sat May 28 00:00:00 BST 2022

REPOSITORIES: jPOST

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pSNAP: Proteome-wide analysis of elongating nascent polypeptide chains.

Uchiyama Junki J Roy Rohini R Wang Dan Ohtan DO Morikawa Kazuya K Kawahara Yuka Y Iwasaki Mio M Yoshino Chiaki C Mishima Yuichiro Y Ishihama Yasushi Y Imami Koshi K

iScience 20220603 7

Cellular global translation is often measured using ribosome profiling or quantitative mass spectrometry, but these methods do not provide direct information at the level of elongating nascent polypeptide chains (NPCs) and associated co-translational events. Here, we describe pSNAP, a method for proteome-wide profiling of NPCs by affinity enrichment of puromycin- and stable isotope-labeled polypeptides. pSNAP does not require ribosome purification and/or chemical labeling, and captures <i>bona f ...[more]

PMID: 35754732

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