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. 2024 Aug 14;43(19):4324–4355. doi: 10.1038/s44318-024-00194-2

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© The Author(s) 2024

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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(A) Protein alignment of the N-terminus of human Cyclin B1 with known arginine anchors of other nucleosome interacting proteins. (B) Protein alignment of the N-terminus of Cyclin B1 orthologues. (C) Quantification of EMSAs of full-length Cyclin B1^WT and the indicated Cyclin B1 variants. N = 3 independent experiments. Mean ± standard deviation are plotted. (D) Cryo-EM structure of the NCP in complex with Cyclin B N-terminus (NCP^CbNT). On the left, the cryo-EM density is low-pass filtered to 7 Å to show the nucleosome particle in its entirety (including the less rigid entry and exit DNA). On the right, the same structure is shown at full power (2.5 Å resolution). (E) A close-up view of D, residues 2–4 of Cyclin B1 interact with the acidic patch of NCP147. Cyclin B1 is shown as a ball and stick, histones H2A and H2B are shown as electrostatic surface potentials (−/+5.000). (F) Same structure as in (E), however, H2A and H2B histones are shown as ribbon models. Interacting side chains are depicted. Dashed lines indicate hydrogen bonds between R4 of Cyclin B1 and acidic patch residues D90 and E92. Cyclin B1 peptide backbone at A2 interacts with E110 of H2B. (G) Cryo-EM density on the side chains shown in (F). (H) Maximum projections of confocal images representative of RPE-1 Cyclin B1-mEmerald^+/+ cells ectopically expressing the indicated variant of Cyclin B1-mScarlet. The scale bar represents 10 μm. (I) Line-profile graph representing the pixel-by-pixel fluorescence intensity over a line drawn from centrosome to centrosome of RPE-1 Cyclin B1-mEmerald^+/+ cells ectopically expressing the indicated Cyclin B1 variant: n = 18 cells per condition, N = 3 independent experiments. Mean ± standard deviation are plotted. (J) Line-profile graph representing the pixel-by-pixel fluorescence intensity over a line drawn from centrosome to centrosome of RPE-1 Cyclin B1-mEmerald^+/+ cells ectopically expressing the indicated Securin variant: n ≥ 16 cells per condition, N = 3 independent experiments. Mean ± standard deviation are plotted. Source data are available online for this figure.