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Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition
During the maternal-to-zygotic transition (MZT), maternal proteins in oocytes are degraded by the ubiquitin–proteasome system (UPS), and new proteins are synthesized from the zygotic genome. However, the specific mechanisms underlying the UPS at the MZT are not well understood. We identified a molec...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575651/ https://www.ncbi.nlm.nih.gov/pubmed/23429752 http://dx.doi.org/10.1242/bio.20123020 |
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author | Shin, Seung-Wook Shimizu, Natsumi Tokoro, Mikiko Nishikawa, Satoshi Hatanaka, Yuki Anzai, Masayuki Hamazaki, Jun Kishigami, Satoshi Saeki, Kazuhiro Hosoi, Yoshihiko Iritani, Akira Murata, Shigeo Matsumoto, Kazuya |
author_facet | Shin, Seung-Wook Shimizu, Natsumi Tokoro, Mikiko Nishikawa, Satoshi Hatanaka, Yuki Anzai, Masayuki Hamazaki, Jun Kishigami, Satoshi Saeki, Kazuhiro Hosoi, Yoshihiko Iritani, Akira Murata, Shigeo Matsumoto, Kazuya |
author_sort | Shin, Seung-Wook |
collection | PubMed |
description | During the maternal-to-zygotic transition (MZT), maternal proteins in oocytes are degraded by the ubiquitin–proteasome system (UPS), and new proteins are synthesized from the zygotic genome. However, the specific mechanisms underlying the UPS at the MZT are not well understood. We identified a molecule named zygote-specific proteasome assembly chaperone (ZPAC) that is specifically expressed in mouse gonads, and expression of ZPAC was transiently increased at the mouse MZT. ZPAC formed a complex with Ump1 and associated with precursor forms of 20S proteasomes. Transcription of ZPAC genes was also under the control of an autoregulatory feedback mechanism for the compensation of reduced proteasome activity similar to Ump1 and 20S proteasome subunit gene expression. Knockdown of ZPAC in early embryos caused a significant reduction of proteasome activity and decrease in Ump1 and mature proteasomes, leading to accumulation of proteins that need to be degraded at the MZT and early developmental arrest. Therefore, a unique proteasome assembly pathway mediated by ZPAC is important for progression of the mouse MZT. |
format | Online Article Text |
id | pubmed-3575651 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The Company of Biologists |
record_format | MEDLINE/PubMed |
spelling | pubmed-35756512013-02-21 Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition Shin, Seung-Wook Shimizu, Natsumi Tokoro, Mikiko Nishikawa, Satoshi Hatanaka, Yuki Anzai, Masayuki Hamazaki, Jun Kishigami, Satoshi Saeki, Kazuhiro Hosoi, Yoshihiko Iritani, Akira Murata, Shigeo Matsumoto, Kazuya Biol Open Research Article During the maternal-to-zygotic transition (MZT), maternal proteins in oocytes are degraded by the ubiquitin–proteasome system (UPS), and new proteins are synthesized from the zygotic genome. However, the specific mechanisms underlying the UPS at the MZT are not well understood. We identified a molecule named zygote-specific proteasome assembly chaperone (ZPAC) that is specifically expressed in mouse gonads, and expression of ZPAC was transiently increased at the mouse MZT. ZPAC formed a complex with Ump1 and associated with precursor forms of 20S proteasomes. Transcription of ZPAC genes was also under the control of an autoregulatory feedback mechanism for the compensation of reduced proteasome activity similar to Ump1 and 20S proteasome subunit gene expression. Knockdown of ZPAC in early embryos caused a significant reduction of proteasome activity and decrease in Ump1 and mature proteasomes, leading to accumulation of proteins that need to be degraded at the MZT and early developmental arrest. Therefore, a unique proteasome assembly pathway mediated by ZPAC is important for progression of the mouse MZT. The Company of Biologists 2012-11-23 /pmc/articles/PMC3575651/ /pubmed/23429752 http://dx.doi.org/10.1242/bio.20123020 Text en © 2012. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by-nc-sa/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial Share Alike License (http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Article Shin, Seung-Wook Shimizu, Natsumi Tokoro, Mikiko Nishikawa, Satoshi Hatanaka, Yuki Anzai, Masayuki Hamazaki, Jun Kishigami, Satoshi Saeki, Kazuhiro Hosoi, Yoshihiko Iritani, Akira Murata, Shigeo Matsumoto, Kazuya Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition |
title | Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition |
title_full | Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition |
title_fullStr | Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition |
title_full_unstemmed | Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition |
title_short | Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition |
title_sort | mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575651/ https://www.ncbi.nlm.nih.gov/pubmed/23429752 http://dx.doi.org/10.1242/bio.20123020 |
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