Degradation of the separase-cleaved REC8, a meiotic cohesin subunit, by the N-end rule pathway
dc.contributor.author | Liu, Yu-Jiao | |
dc.contributor.author | Chang, ZeNan | |
dc.contributor.author | Wadas, Brandon | |
dc.contributor.author | Brower, Christopher S. | |
dc.contributor.author | Song, Zhen-Hua | |
dc.contributor.author | Xu, Zhi-Liang | |
dc.contributor.author | Shang, Yong-Liang | |
dc.contributor.author | Liu, Wei-Xiao | |
dc.contributor.author | Wang, Li-Na | |
dc.contributor.author | Dong, Wen | |
dc.contributor.author | Varshavsky, Alexander | |
dc.contributor.author | Hu, Rong-Gui | |
dc.contributor.author | Li, Wei | |
dc.creator.orcid | https://orcid.org/0000-0003-0289-5541 | |
dc.date.accessioned | 2023-01-20T16:30:05Z | |
dc.date.available | 2023-01-20T16:30:05Z | |
dc.date.issued | 2016 | |
dc.description.abstract | The Ate1 arginyltransferase (R-transferase) is a component of the N-end rule pathway, which recognizes proteins containing N-terminal degradation signals called N-degrons, polyubiquitylates these proteins, and thereby causes their degradation by the proteasome. Ate1 arginylates N-terminal Asp, Glu, or (oxidized) Cys. The resulting N-terminal Arg is recognized by ubiquitin ligases of the N-end rule pathway. In the yeast Saccharomyces cerevisiae, the separase-mediated cleavage of the Scc1/Rad21/Mcd1 cohesin subunit generates a C-terminal fragment that bears N-terminal Arg and is destroyed by the N-end rule pathway without a requirement for arginylation. In contrast, the separase-mediated cleavage of Rec8, the mammalian meiotic cohesin subunit, yields a fragment bearing N-terminal Glu, a substrate of the Ate1 R-transferase. Here we constructed and used a germ cell-confined Ate1−/− mouse strain to analyze the separase-generated C-terminal fragment of Rec8. We show that this fragment is a short-lived N-end rule substrate, that its degradation requires N-terminal arginylation, and that male Ate1−/− mice are nearly infertile, due to massive apoptotic death of Ate1−/− spermatocytes during the metaphase of meiosis I. These effects of Ate1 ablation are inferred to be caused, at least in part, by the failure to destroy the C-terminal fragment of Rec8 in the absence of N-terminal arginylation. | en_US |
dc.identifier.citation | This is the published version of an article that is available at https://doi.org/10.1074/jbc.m116.714964. Recommended citation: Liu, Y.-J., Liu, C., Chang, Z. N., Wadas, B., Brower, C. S., Song, Z.-H., Xu, Z.-L., Shang, Y.-L., Liu, W.-X., Wang, L.-N., Dong, W., Varshavsky, A., Hu, R.-G., & Li, W. (2016). Degradation of the separase-cleaved REC8, a meiotic cohesin subunit, by the N-end rule pathway. Journal of Biological Chemistry, 291(14), 7426–7438. This item has been deposited in accordance with publisher copyright and licensing terms and with the author’s permission. | en_US |
dc.identifier.uri | https://hdl.handle.net/11274/14334 | |
dc.identifier.uri | https://doi.org/10.1074/jbc.m116.714964 | |
dc.language.iso | en_US | en_US |
dc.publisher | Elsevier | en_US |
dc.rights.license | CC-BY 4.0 | |
dc.subject | Meiosis | en_US |
dc.subject | Protein degradation | en_US |
dc.subject | Proteolysis | en_US |
dc.subject | Spermatogenesis | en_US |
dc.subject | Ubiquitin | en_US |
dc.title | Degradation of the separase-cleaved REC8, a meiotic cohesin subunit, by the N-end rule pathway | en_US |
dc.type | Article | en_US |
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