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. 2021 Jul 14;12:4322. doi: 10.1038/s41467-021-24554-2

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© The Author(s) 2021

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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Fig. 2 — a Mean VFP-tagged securin FL (purple dashed trace, n = 11) destruction profile following incubation in 1.5 µM ProTAME to inhibit APC/C activity. Mean VFP-tagged securin FL (magenta trace, n = 16) destruction profile in control oocytes is included as a reference. ProTAME treated oocytes do not extrude a polar body and are therefore aligned at GVBD. b Schematic showing VFP-tagged securin and cyclin B1 constructs. c Mean securin FL (magenta trace, n = 25), securin N101 (pink dashed trace, n = 23), cyclin B1 FL (blue trace, n = 33) and cyclin B1 N90 (light blue dashed trace, n = 34) destruction profiles relative to PB1 extrusion. d Full sequence alignment conservation annotation and multiple sequence alignment of residues 109–133 in securin orthologs. e Mean VFP-tagged securin FL (magenta trace, n = 25), securin N101 (pink dashed trace, n = 23) and securin Δ109–133 (light blue trace, n = 23) destruction profiles relative to PB1 extrusion. f Schematic showing the position of Securin FF-A amino-acid substitutions. Residues F125 and F128 (shown in green in the wild-type protein) were switched to alanines (shown in red in Securin FF-A). g Mean VFP-tagged securin FL (magenta trace, n = 25), securin N101 (pink dashed trace, n = 23) and securin FF-A (green trace, n = 20) destruction traces relative to PB1 extrusion. h Mean VFP-tagged securin FL (magenta dashed trace, n = 23) and securin FF-A (dark green dashed trace, n = 30) destruction profiles following incubation in 150 nM nocodazole to arrest oocytes in prometaphase. Mean VFP-tagged securin FL (magenta trace, n = 16) and securin FF-A (green trace, n = 16) destruction profiles in control oocytes are included as a reference. Nocodazole treated oocytes do not extrude a polar body and are therefore aligned at GVBD. i Mean VFP-tagged securin FL (purple dashed trace, n = 16) and securin FF-A (dark green dashed trace, n = 16) destruction profiles following incubation in 100 nM reversine to block assembly of new SAC complexes. Mean VFP-tagged securin FL (magenta trace, n = 16) and securin FF-A (green trace, n = 16) destruction profiles in control oocytes are included as a reference. Reversine treated oocytes have an accelerated progression through meiosis and are therefore aligned at GVBD. All n numbers refer to the number of individual oocytes analysed over a minimum of three independent experiments. All error bars ± SEM.