Post-testicular spermatozoa of a marine teleost can conduct de novo cytoplasmic and mitochondrial translation
Júlia Castro-Arnau,
François Chauvigné,
Asier González,
Roderick Nigel Finn,
Montserrat Carrascal,
Joan Cerdà
Affiliations
Júlia Castro-Arnau
Institute of Marine Sciences, Spanish National Research Council (CSIC), 08003 Barcelona, Spain; Institute of Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
François Chauvigné
Institute of Marine Sciences, Spanish National Research Council (CSIC), 08003 Barcelona, Spain; Institute of Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
Asier González
Institute of Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
Roderick Nigel Finn
Institute of Marine Sciences, Spanish National Research Council (CSIC), 08003 Barcelona, Spain; Institute of Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain; Department of Biological Sciences, University of Bergen, 5020 Bergen, Norway
Montserrat Carrascal
Biological and Environmental Proteomics Group, Institute of Biomedical Research of Barcelona, Spanish National Research Council (IIBB-CSIC/IDIBAPS), 08036 Barcelona, Spain
Joan Cerdà
Institute of Marine Sciences, Spanish National Research Council (CSIC), 08003 Barcelona, Spain; Institute of Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain; Corresponding author
Summary: Translational silence of spermatozoa has long been considered the norm in animals. However, studies in mammals have shown that the mitochondrial ribosomal machinery is selectively activated during capacitation in the female reproductive tract, while cytosolic ribosomes remain inactive. Here, using quantitative proteomics in a piscine model species, we show that proteins involved in mRNA processing and cytoplasmic translation are predominantly accumulated in immature spermatozoa within the extratesticular excurrent ducts, while those related to flagellar motility are enriched in ejaculated (mature) sperm. Based upon in vitro incubation of isolated spermatozoa, motility assays and polysome profiling, we further show that 80S cytoplasmic and 55S mitochondrial ribosomes are actively involved in the translation of motility- and osmoadaptation-related proteins. These findings thus reveal that post-testicular piscine spermatozoa can maintain de novo protein synthesis through both mitochondrial and cytoplasmic ribosomal activity, which is necessary for the acquisition of full sperm function.
