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. 2017 Dec 18;7:17742. doi: 10.1038/s41598-017-18009-2

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© The Author(s) 2017

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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Functional characterization of the putative EsCLK:EsCYC/BMAL’s inhibitors. (A,B) EsCRY1 and EsCRY2 functional validation by luciferase assay in S2R + and HEK293 cells, respectively. Cells were transfected with indicated constructs. Negative control set as 1. Data are represented as mean ± SEM (n = 3 independent transfections). (C) Western blot and relative quantification of EsCRY1 protein in the dark and after a 8 hours light pulse in Drosophila cells. Data are represented as mean ± SD (n = 3 independent transfections). NC: negative control. (D,E) Comparison of the effectiveness of EsPER, EsTIM1, and EsCRY2 for inhibiting the transcription of the E-box/luciferase reporter mediated by the EsCLK:EsCYC/BMAL dimer in S2R + and HEK293 cells respectively. S2R + and HEK293 cells were transfected with the indicated constructs. Negative control set as 1. Data are represented as mean ± SD (n = 3 independent transfections). (F) Co-immonoprecipitation of EsCRY2 and EsCYC/BMAL quantified by luciferase assay. EsCyc/Bmal C-terminally fused to luciferase (EsCyc/Bmal-LUC) was co-immunoprecipitated with EsCry2-V5 and anti-V5 antidody in HEK293 cells. Data are presented as mean ± SD (n = 3 independent transfections). Student’s t-test Bonferroni-corrected p-values for all the experimental comparisons discussed were presented in Supplementary Table 3. Statistical significance of the most relevant comparisons were shown as *p < 0.05, **p < 0.01, and ***p < 0.005.