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. 2019 Sep 20;9:13618. doi: 10.1038/s41598-019-50052-z

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Identification of proteins associated with Tnp1 and Tnp2 mRNAs. (a) Schematic diagram of Tnp mRNA/protein complex isolation. Biotinylated (red) DNA oligonucleotides were captured onto strepatavidin beads (yellow) and then incubated with testis lysate to bind Tnp mRNAs with associated proteins (green). After washing to remove unbound mRNAs and proteins, endogenous Tnp mRNA/protein complexes were eluted with an excess of complementary oligonucleotide (purple) and subsequently analyzed. (b) Tnp mRNAs are present in both inactive and actively translated mRNA fractions. A representative polysome profile analysis of adult mouse testis extract is shown (top), detecting the presence of ribosomal subunits (40S and 60S), monosomes (80S), and polysomes by UV absorbance (254 nm). Three biological replicates were performed. Tnp1, Tnp2 and Actin mRNAs in sucrose gradient fractions were analyzed using RT-qPCR (bottom). The data are plotted as the percentage of the particular mRNA in a fraction relative to the sum across all gradient fractions. Error bars represent the SEM for the three biological replicates.