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The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition
KAT6 histone acetyltransferases (HATs) are highly conserved in eukaryotes and are involved in cell cycle regulation. However, information regarding their roles in regulating cell cycle progression is limited. Here, we report the identification of subunits of the Drosophila Enok complex and demonstra...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4888840/ https://www.ncbi.nlm.nih.gov/pubmed/27198229 http://dx.doi.org/10.1101/gad.271429.115 |
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author | Huang, Fu Saraf, Anita Florens, Laurence Kusch, Thomas Swanson, Selene K. Szerszen, Leanne T. Li, Ge Dutta, Arnob Washburn, Michael P. Abmayr, Susan M. Workman, Jerry L. |
author_facet | Huang, Fu Saraf, Anita Florens, Laurence Kusch, Thomas Swanson, Selene K. Szerszen, Leanne T. Li, Ge Dutta, Arnob Washburn, Michael P. Abmayr, Susan M. Workman, Jerry L. |
author_sort | Huang, Fu |
collection | PubMed |
description | KAT6 histone acetyltransferases (HATs) are highly conserved in eukaryotes and are involved in cell cycle regulation. However, information regarding their roles in regulating cell cycle progression is limited. Here, we report the identification of subunits of the Drosophila Enok complex and demonstrate that all subunits are important for its HAT activity. We further report a novel interaction between the Enok complex and the Elg1 proliferating cell nuclear antigen (PCNA)-unloader complex. Depletion of Enok in S2 cells resulted in a G1/S cell cycle block, and this block can be partially relieved by depleting Elg1. Furthermore, depletion of Enok reduced the chromatin-bound levels of PCNA in both S2 cells and early embryos, suggesting that the Enok complex may interact with the Elg1 complex and down-regulate its PCNA-unloading function to promote the G1/S transition. Supporting this hypothesis, depletion of Enok also partially rescued the endoreplication defects in Elg1-depleted nurse cells. Taken together, our study provides novel insights into the roles of KAT6 HATs in cell cycle regulation through modulating PCNA levels on chromatin. |
format | Online Article Text |
id | pubmed-4888840 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-48888402016-11-15 The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition Huang, Fu Saraf, Anita Florens, Laurence Kusch, Thomas Swanson, Selene K. Szerszen, Leanne T. Li, Ge Dutta, Arnob Washburn, Michael P. Abmayr, Susan M. Workman, Jerry L. Genes Dev Research Paper KAT6 histone acetyltransferases (HATs) are highly conserved in eukaryotes and are involved in cell cycle regulation. However, information regarding their roles in regulating cell cycle progression is limited. Here, we report the identification of subunits of the Drosophila Enok complex and demonstrate that all subunits are important for its HAT activity. We further report a novel interaction between the Enok complex and the Elg1 proliferating cell nuclear antigen (PCNA)-unloader complex. Depletion of Enok in S2 cells resulted in a G1/S cell cycle block, and this block can be partially relieved by depleting Elg1. Furthermore, depletion of Enok reduced the chromatin-bound levels of PCNA in both S2 cells and early embryos, suggesting that the Enok complex may interact with the Elg1 complex and down-regulate its PCNA-unloading function to promote the G1/S transition. Supporting this hypothesis, depletion of Enok also partially rescued the endoreplication defects in Elg1-depleted nurse cells. Taken together, our study provides novel insights into the roles of KAT6 HATs in cell cycle regulation through modulating PCNA levels on chromatin. Cold Spring Harbor Laboratory Press 2016-05-15 /pmc/articles/PMC4888840/ /pubmed/27198229 http://dx.doi.org/10.1101/gad.271429.115 Text en © 2016 Huang et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/. |
spellingShingle | Research Paper Huang, Fu Saraf, Anita Florens, Laurence Kusch, Thomas Swanson, Selene K. Szerszen, Leanne T. Li, Ge Dutta, Arnob Washburn, Michael P. Abmayr, Susan M. Workman, Jerry L. The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition |
title | The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition |
title_full | The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition |
title_fullStr | The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition |
title_full_unstemmed | The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition |
title_short | The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition |
title_sort | enok acetyltransferase complex interacts with elg1 and negatively regulates pcna unloading to promote the g1/s transition |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4888840/ https://www.ncbi.nlm.nih.gov/pubmed/27198229 http://dx.doi.org/10.1101/gad.271429.115 |
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