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Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation

Histone deacetylation plays an important role in transcriptional repression. Previous results showed that the genetic interaction between ttk and rpd3, which encodes a class I histone deacetylase, is required for tll repression. This study investigated the molecular mechanism by which Ttk69 recruits...

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Autor principal: Liaw, Gwo-Jen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5020733/
https://www.ncbi.nlm.nih.gov/pubmed/27622813
http://dx.doi.org/10.1038/srep33388
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author Liaw, Gwo-Jen
author_facet Liaw, Gwo-Jen
author_sort Liaw, Gwo-Jen
collection PubMed
description Histone deacetylation plays an important role in transcriptional repression. Previous results showed that the genetic interaction between ttk and rpd3, which encodes a class I histone deacetylase, is required for tll repression. This study investigated the molecular mechanism by which Ttk69 recruits Rpd3. Using yeast two-hybrid screening and datamining, one novel protein was found that weakly interacts with Ttk69 and Sin3A, designated as Protein interacting with Ttk69 and Sin3A (Pits). Pits protein expressed in the early stages of embryos and bound to the region of the tor response element in vivo. Expanded tll expression patterns were observed in embryos lacking maternal pits activity and the expansion was not widened by reducing either maternal ttk or sin3A activity. However, in embryos with simultaneously reduced maternal pits and sin3A activities or maternal pits, sin3A and ttk activities, the proportions of the embryos with expanded tll expression were significantly increased. These results indicate that all three gene activities are involved in tll repression. Level of histone H3 acetylation in the tll proximal region was found to be elevated in embryo with reduced these three gene activities. In conclusion, Ttk69 causes the histone deacetylation-mediated repression of tll via the interaction of Pits and Sin3A.
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spelling pubmed-50207332016-09-20 Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation Liaw, Gwo-Jen Sci Rep Article Histone deacetylation plays an important role in transcriptional repression. Previous results showed that the genetic interaction between ttk and rpd3, which encodes a class I histone deacetylase, is required for tll repression. This study investigated the molecular mechanism by which Ttk69 recruits Rpd3. Using yeast two-hybrid screening and datamining, one novel protein was found that weakly interacts with Ttk69 and Sin3A, designated as Protein interacting with Ttk69 and Sin3A (Pits). Pits protein expressed in the early stages of embryos and bound to the region of the tor response element in vivo. Expanded tll expression patterns were observed in embryos lacking maternal pits activity and the expansion was not widened by reducing either maternal ttk or sin3A activity. However, in embryos with simultaneously reduced maternal pits and sin3A activities or maternal pits, sin3A and ttk activities, the proportions of the embryos with expanded tll expression were significantly increased. These results indicate that all three gene activities are involved in tll repression. Level of histone H3 acetylation in the tll proximal region was found to be elevated in embryo with reduced these three gene activities. In conclusion, Ttk69 causes the histone deacetylation-mediated repression of tll via the interaction of Pits and Sin3A. Nature Publishing Group 2016-09-13 /pmc/articles/PMC5020733/ /pubmed/27622813 http://dx.doi.org/10.1038/srep33388 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Liaw, Gwo-Jen
Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation
title Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation
title_full Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation
title_fullStr Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation
title_full_unstemmed Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation
title_short Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation
title_sort pits, a protein interacting with ttk69 and sin3a, has links to histone deacetylation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5020733/
https://www.ncbi.nlm.nih.gov/pubmed/27622813
http://dx.doi.org/10.1038/srep33388
work_keys_str_mv AT liawgwojen pitsaproteininteractingwithttk69andsin3ahaslinkstohistonedeacetylation