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. 2018 Dec 6;16:144. doi: 10.1186/s12915-018-0613-5

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© The Author(s). 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 2 — 2c-Cyclops possess cytosolic N-termini and a likely 8 transmembrane helices topology. a Schematic model of BiFC (bimolecular fluorescence complementation) experiments. The opsin domain was N- and C-terminally fused to the two parts of split YFP (YFP_C = aa155–238 of YFP, YFP_N = aa1–154 of YFP). b Fluorescence pictures show the following: control oocyte (control), oocytes expressing YFP_C::Cr2c-Cyclop1/opsin::YFP_N (Cr2c-Cyclop1), YFP_C::Vc2c-Cyclop1/opsin::YFP_N (Vc2c-Cyclop1), and YFP_C::Cop5/opsin::YFP_N (Cop5(HKR)) constructs. The fusion sequence of YFP_C and YFP_N was designed according to the YFP structure to facilitate the fluorescence complementation. The fluorescence images were taken by a confocal microscope 3 dpi (days post injection) with 30 ng cRNA injection into Xenopus oocytes. Scale bars 250 μm