In Depth Exploration of the Alternative Proteome of Drosophila melanogaster

Frontiers in Cell and Developmental Biology

Sebastien A. Choteau¹  Christine Brun²  Bertrand Fabre³  Michael J. Deery³  Kathryn S. Lilley³  Steven Russell⁴  Dagmara Korona⁴  Carole Pichereaux⁶  Odile Burlet-Schiltz⁶  Mylène Camus⁶  Carine Duboé⁸  Audrey Montigny⁸  Serge Plaza⁸  Jean-Philippe Combier⁸ 

[1] Aix-Marseille Université, INSERM, TAGC, Turing Centre for Living Systems, Marseille, France;CNRS, Marseille, France;Cambridge Centre for Proteomics, Cambridge Systems Biology Centre and Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom;Cambridge Systems Biology Centre and Department of Genetics, University of Cambridge, Cambridge, United Kingdom;Fédération de Recherche (FR3450), Agrobiosciences, Interactions et Biodiversité (AIB), CNRS, Toulouse, France;Infrastructure Nationale de Protéomique, ProFI, FR 2048, Toulouse, France;Institut de Pharmacologie et de Biologie Structurale (IPBS), Université de Toulouse, CNRS, UPS, Toulouse, France;Laboratoire de Recherche en Sciences Végétales, UMR5546, Université de Toulouse, UPS, INP, CNRS, Auzeville-Tolosane, France;

关键词: alternative proteins;    short open reading frame–encoded polypeptide;    microprotein;    peptidomics;    mass spectrometry;   

DOI  :  10.3389/fcell.2022.901351

来源: DOAJ

【 摘 要 】

Recent studies have shown that hundreds of small proteins were occulted when protein-coding genes were annotated. These proteins, called alternative proteins, have failed to be annotated notably due to the short length of their open reading frame (less than 100 codons) or the enforced rule establishing that messenger RNAs (mRNAs) are monocistronic. Several alternative proteins were shown to be biologically active molecules and seem to be involved in a wide range of biological functions. However, genome-wide exploration of the alternative proteome is still limited to a few species. In the present article, we describe a deep peptidomics workflow which enabled the identification of 401 alternative proteins in Drosophila melanogaster. Subcellular localization, protein domains, and short linear motifs were predicted for 235 of the alternative proteins identified and point toward specific functions of these small proteins. Several alternative proteins had approximated abundances higher than their canonical counterparts, suggesting that these alternative proteins are actually the main products of their corresponding genes. Finally, we observed 14 alternative proteins with developmentally regulated expression patterns and 10 induced upon the heat-shock treatment of embryos, demonstrating stage or stress-specific production of alternative proteins.

【 授权许可】

Unknown