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Ribosomal protein signature in adult mouse organs

ABSTRACT: we purified the ribosomal fraction from 14 different adult mouse tissues and analyzed their protein composition using quantitative mass spectrometry (MS)-based proteomics. We show that ribosomes exhibit heterogeneity in RP composition, not only in the case of RP paralogues (e.g. in muscle and testis, consistent with previous research), but also for several unexpected RPs displaying variability among different organs.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Heart, Cerebellum, Testis, Spleen, Brain, Skeletal Muscle, Liver, Lung, Retina, Adrenal Gland, Kidney, Small Intestine

SUBMITTER: Hesse Anne-Marie

LAB HEAD: Yohann Couté

PROVIDER: PXD044060 | Pride | 2025-05-06

REPOSITORIES: Pride

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			Action	DRS
	EXPORT.mzid.gz	Mzid
	HF1_008817.mgf	Mgf
	HF1_008817.raw	Raw
	HF1_008819.mgf	Mgf
	HF1_008819.raw	Raw

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Publications

Proteomics-based characterization of ribosome heterogeneity in adult mouse organs.

Brunchault Marie R MR Hesse Anne-Marie AM Schaeffer Julia J Fröhlich Albrecht A Saintpierre Ana A Decourt Charlotte C Combes Florence F Nawabi Homaira H Couté Yohann Y Belin Stephane S

Cellular and molecular life sciences : CMLS 20250424 1

The translation process, leading to protein synthesis from mRNA, has been long thought to be invariable in all cellular organisms. Increasing evidence shows that it is finely regulated by variable features of the translation machinery. Notably, ribosomes, the functional units of protein synthesis, are suggested to display variations in their composition, depending on the developmental stage, cell type or physio-pathological context, thus hinting a new level of actionable regulation of gene expre ...[more]

PMID: 40272563

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