Abstract
The kinetochore is the crucial apparatus regulating chromosome segregation in mitosis and meiosis. Particularly in meiosis I, unlike in mitosis, sister kinetochores are captured by microtubules emanating from the same spindle pole (mono-orientation) and centromeric cohesion mediated by cohesin is protected in the following anaphase. Although meiotic kinetochore factors have been identified only in budding and fission yeasts, these molecules and their functions are thought to have diverged earlier. Therefore, a conserved mechanism for meiotic kinetochore regulation remains elusive. Here we have identified in mouse a meiosis-specific kinetochore factor that we termed MEIKIN, which functions in meiosis I but not in meiosis II or mitosis. MEIKIN plays a crucial role in both mono-orientation and centromeric cohesion protection, partly by stabilizing the localization of the cohesin protector shugoshin. These functions are mediated mainly by the activity of Polo-like kinase PLK1, which is enriched to kinetochores in a MEIKIN-dependent manner. Our integrative analysis indicates that the long-awaited key regulator of meiotic kinetochore function is Meikin, which is conserved from yeasts to humans.
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Acknowledgements
We thank K. Tachibana-Konwalski for the C57BL/6 Mlh1tm1Liskay knockout mice and and J. Ellenberg for a macro for automated microscopy. We also thank J. Lee, T. Hirano, S. Fujiyama, Y. Yamazumi, as well as the Gotoh laboratory for technical advice and all members of the Watanabe laboratory for their support and discussion. This work was supported in part by a JSPS Research Fellowship (to J.K.), SAF2011-25252 (to A.M.P.), a research grant from Uehara Memorial Foundation, a RIKEN CDB intramural grant and a Grant-in-Aid for Young Scientists (B) (to T.S.K.), a Grant-in-Aid for Scientific Research on Innovative Areas, a Grant-in-Aid for Scientific Research (C) (to K.I.), and a Grant-in-Aid for Specially Promoted Research (to Y.W.) from MEXT, Japan.
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J.K., supported by K.I. performed most of the experiments in mice. K.I. and N.T. generated Meikin knockout mice. A.M.P. provided Sgo2 knockout mice. A.N. isolated MEIKIN in yeast two-hybrid screening. B.A., S.Y., A.K., T.I. and T.S. performed experiments in fission yeast. Y.S. and T.S.K. performed live imaging. The experimental design and interpretation of data were conducted by J.K., K.I., B.A., S.Y., A.K., T.I., T.S.K., Y.T. and T.S. Y.W. supervised the project, and wrote the paper with input from all authors.
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Extended data figures and tables
Extended Data Figure 1 MEIKIN (4930404A10rik) was identified as a meiosis-specific CENP-C binding protein.
a, Yeast two-hybrid screening was performed using CENP-C C terminus (amino acids 692–906) as bait and a mouse testis cDNA library as prey. A total of 11.95 × 107 colonies were screened on selective (SD-Trp-Leu-His-Ade, +10 mM 3AT) plates using the AH109 tester strain. The number of clones isolated by screening is summarized. b, To search for a meiosis-specific candidate from the isolated clones, tissue-specific expression patterns of CENP-C interactors were examined by RT–PCR. RNA was extracted from each tissue of both males and females. Testis RNA was derived from 8-week-old males. Ovary RNA was derived from 4- and 8-week-old females. RT(−) indicates control PCR without reverse transcription. Note that the expression of 4930404A10rik is restricted to testis and ovary, as is that of SMC1β. c, Immunoprecipitates from mouse testis chromatin extracts using anti-CENP-C antibody or control IgG were analysed by the indicated antibody. d, The C-terminal domain of MEIKIN (4930404A10rik) (amino acids 385–434) interacts with the CENP-C C terminus in yeast two-hybrid assay.
Extended Data Figure 2 Sequence alignment of MEIKIN homologues in vertebrates.
Amino acid sequences of M. musculus 4930404A10Rik (NP_083381), R. norvegicus (XP_573090), C. lupus (XP_003639413), X. tropicalis (XP_002934413) and G. gallus (XP_001234011) are derived from the NCBI protein database. H. sapiens data are derived from cDNA clones. 4930404A10Rik protein is conserved among vertebrates but it does not have any known motif except for the polo-box binding motif (blue line) in mammalian proteins. Two-hybrid assays indicate that this motif of mouse MEIKIN is important for PLK1 binding (data not shown), although the motif is apparently not conserved in Xenopus and chicken. The C-terminal sequences (red lines) are required for the kinetochore localization (see Fig. 1c).
Extended Data Figure 3 Co-localization of CENP-C and ACA in spermatocytes and MEKIN localization in oocytes.
a, Squashed spermatocytes from wild-type were immunostained for CENP-C, ACA, SYCP3 and DAPI at the indicated stages during meiosis. CENP-C and ACA signals accumulate and co-localize at centromeres after zygotene throughout meiosis. b, Chromosome spreads of oocytes from wild-type were immunostained for MEIKIN, ACA and REC8 at different meiotic stages. Zygotene from E15.5, pachytene and diplotene from E18.5 mice. c, Chromosome spreads of oocytes at metaphase I (5 h after GVBD) and metaphase II (16 h post GVBD) were stained for MEIKIN, ACA and DAPI. Scale bars, 5 μm.
Extended Data Figure 4 Generation of Meikin-knockout mice.
a, Schematic illustrations of the wild-type allele and targeted Meikin−/− allele are shown. Grey boxes represent exons. The targeted exon 4 contains the intact splicing acceptor (SA) sequence followed by a premature stop codon, resulting in disruption of the Meikin allele. Black bar probe for Southern blot. b, Southern blot of genomic DNA from wild type (+/+) and Meikin heterozygous (+/−) ES cells after Pvu II digestion. ES cell clone number 2 used to generate the mice. c, Immunoblot analysis of testis extracts prepared from mice with the indicated genotypes (4-week-old). In Meikin−/−, the specific bands probed by the anti-MEIKIN antibody are absent (shown as arrowheads). α-tubulin is a loading control. d, Testes from 12-week-old wild-type (+/+) and Meikin−/− (−/−) mice. e, Haematoxylin and eosin staining of a section of the testis (12-week-old) showed seminiferous tubules. Enlarged pictures of seminiferous tubules showed spermatocyte (black arrowheads) and spermatids (yellow arrowheads) in wild-type and Meikin−/−. Scale bar, 100 μm. f, Haematoxylin-eosin staining of epididymis from 12-week-old mice shows reduced number of sperms in Meikin−/ −. Enlarged images of sperms are shown. Scale bar, 50 μm. g, A pair of ovaries (8-week-old) from the indicated genotypes (top). Haematoxylin and eosin–stained paraffin sections of ovaries from 8-week-old wild-type and Meikin−/− mice (middle). The antral-stage follicles with oocyte nuclei are magnified (bottom). Asterisks indicate corpora lutea. Scale bar, 500 μm.
Extended Data Figure 5 The delay of anaphase I onset in Meikin−/− oocytes is suppressed by inactivation of SAC.
Oocytes from wild-type and Meikin−/− mice were cultured after GVBD in the presence of nocodazole (10 μM) or the Mps1 kinase inhibitor reversin (5 μM). The first polar body extrusion (PBE) rates are shown with mean ± s.e.m. from 3 independent experiments. The total number of oocytes is n = 27 in wild-type with nocodazole (7, 10 and 10, respectively), n = 27 for wild-type with reversine (6, 10 and 11. respectively), n = 21 for Meikin−/− with nocodazole (5, 8 and 8, respectively) and n = 23 for Meikin−/− with reversine (7, 8 and 8, respectively).
Extended Data Figure 6 MEIKIN is required for centromeric cohesion protection and mono-orientation in spermatocytes.
a, Squashed spermatocytes at metaphase I (Meta I) were immunostained for SGO2, ACA and DAPI. Partial z-axis projection images of aligned chromosomes are shown with magnified images of a bivalent (top). The signal intensity of SGO2 adjacent to the centromere was quantified and normalized to that of ACA. The relative intensities are shown with mean + s.e.m. from 3 independent experiments (bottom). In each experiment, 15 centromeres from a spermatocyte were quantified (n = 4 cells). b, Squashed spermatocytes at anaphase I (5 μm < segregated DNA mass distance <10 μm) from wild-type, Meikin−/− and Sgo2−/− mice were immunostained for CENP-C, REC8 and DNA (top). A pair of sister kinetochores is magnified. The distance between sister kinetochores was scored and represented in the scatter plot with median (bottom). A total of 15 kinetochores from 5 spermatocytes were measured in each group (n = kinetochore number). c, Squashed spermatocytes at prometaphase I from wild-type and Meikin−/− mice, and MEF cells at prometaphase (prometa) were immunostained for CENP-C and DNA. Pairs of sister kinetochores are magnified. The distances between sister kinetochores were scored and represented in the graph with mean + s.e.m. from three independent experiments (right). Note that, MEF cells sample preparation and sister kinetochore distance measurements were performed same methods with spermatocytes. In each experiment, 10 kinetochores were measured in a cell (n = 5 cells). *P < 0.05, *** P < 0.001, **** P < 0.0001, unpaired t-test (a–c). Scale bars, 5 μm (unless otherwise indicated).
Extended Data Figure 7 PLK1 was identified as a MEIKIN interactor.
a, Yeast two-hybrid screening of mouse MEIKIN interactors was performed using a mouse testis cDNA library. The number of clones isolated by screening is summarized. Because the use of MEIKIN full-length and N-terminal region (amino acids 1–271) as bait resulted in a high background of false positive interactions in yeast two-hybrid screening, we used MEIKIN C terminus (amino acids 272–434) as bait. b, Yeast two-hybrid assay demonstrates that MEIKIN interacts directly with mouse PLK1 through the MEIKIN C-terminal domain (amino acids 272–434). c, Mouse MEIKIN protein was immunoprecipitated from testis chromatin-bound fraction by two different anti-MEIKIN polyclonal antibodies (A and B). The immunoprecipitates underwent two independent LC–MS/MS analyses. Those proteins commonly identified in all the LC–MS/MS analyses are listed with the number of peptide hits in the table. Note that polo-like kinase (PLK1) as well as CENP-C were repeatedly identified in the two-hybrid screening (a) and LC–MS/MS analyses (c).
Extended Data Figure 8 BI 2536 treatment reduces PLK1 kinase activity in oocytes.
a, Schematic illustration of BI 2536 treatment in wild-type oocyte culture (left). Oocytes were treated with DMSO or BI 2536 (100 nM) during the indicated time periods, then washed and released into normal culture medium. The first polar body extrusion ratio (1st PBE) was counted at 10 h after GVBD (right). Error bars, mean ± s.e.m. from 3 independent experiments. The total number of oocytes used for each experiment is shown. b, Wild-type oocytes treated with DMSO or BI 2536 (during 6–7 h after GVBD) were fixed and immunostained for PLK1 substrate pCENP-U, ACA and DAPI at metaphase I (top). The relative pCENP-U intensity normalized to that of ACA is shown in the graph with mean + s.e.m. from 3 independent experiments. In each experiment, 10 kinetochores from an oocyte were quantified (n = 4 cells). **P < 0.01, unpaired t-test. c, Oocytes were treated with DMSO or BI 2536 during the period of 4–6 h after GVBD and stained for α-tubulin, CENP-C and DAPI (DNA) at the indicated stages in whole mount (related to Fig. 4d). Magnified images are shown to highlight the separation of sister kinetochores in BI 2536-treated oocyte in anaphase I. d, Chromosome spreads from control and BI 2536-treated wild-type oocytes at metaphase I (6 h after GVBD) and metaphase II (20 h after GVBD) were stained for REC8, CENP-C and DAPI (DNA) (related to Fig. 4d). Magnified images are shown to highlight the loss of cohesion in BI 2536 treated oocytes in metaphase II. e, Mlh1−/− oocytes (C57BL/6 background) were treated with BI 2536 between 9–10 h after GVBD and stained for α-tubulin, CENP-C and DAPI (DNA) in whole mount (related to Fig. 4e). Magnified images are shown to highlight bi-oriented sister kinetochores at the spindle midzone. Scale bars, 5 μm (unless otherwise indicated).
Extended Data Figure 9 The human homologue of MEIKIN.
a, Schematic illustrations of mouse and human MEIKINs. The putative amino acid sequence of hMEIKIN full-length (373 amino acids) was deduced from our own sequencing of DNA (see Extended Data Fig. 2), which was amplified by RT–PCR from the human testis cDNA. The amino acid sequence equivalent to mouse exon 10 (mEX10) is absent in the hMEIKIN protein, despite our attempts at a computational search to identify the missing DNA sequence. b, Yeast two-hybrid assays demonstrate that the hMEIKIN C terminus interacts with human CENP-C (full length), hCENP-C C-terminal (CENPC motif + Mif2 motif, amino acids 732–945) and hPLK1, in agreement with mouse MEIKIN data. c, Immunostaining of a human seminiferous tubule section (purchased from Biochain) demonstrates that hMEIKIN localizes to centromeres (ACA) in pachytene spermatocytes. We used anti-hMEIKIN-N and anti-hMEIKIN-C antibodies. Enlarged images of the rectangles are shown to highlight the co-localization of ACA and hMEIKIN (bottom). Scale bar, 5 μm.
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: Live imaging of wild-type (WT) and Meikin -/- (KO) oocytes expressing 2mEGFP-CENP-C (green) and H2B-mCherry (red) from metaphase I to anaphase I
Kinetochore signals are peak-enhanced and background-subtracted. Time after the end of metaphase I (min). Scale bar, 10 μm. (AVI 29704 kb)
Live imaging of wild-type (WT) and Meikin -/- (KO) oocytes expressing 2mEGFP-CENP-C (green) and H2B-mCherry (red) from telophase I to metaphase II
Kinetochore signals are peak-enhanced and background-subtracted. Time after telophase I (hh:mm). Scale bar, 10μm. (AVI 25823 kb)
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Kim, J., Ishiguro, Ki., Nambu, A. et al. Meikin is a conserved regulator of meiosis-I-specific kinetochore function. Nature 517, 466–471 (2015). https://doi.org/10.1038/nature14097
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DOI: https://doi.org/10.1038/nature14097
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