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Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena

In this study, we have constructed synthetic peptides which are identical to hyperacetylated amino termini of two Tetrahymena core histones (tetra-acetylated H4 and penta-acetylated hv1) and used them to generate polyclonal antibodies specific for acetylated forms (mono-, di-, tri-, etc.) of these h...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1989
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115542/
https://www.ncbi.nlm.nih.gov/pubmed/2654136
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description In this study, we have constructed synthetic peptides which are identical to hyperacetylated amino termini of two Tetrahymena core histones (tetra-acetylated H4 and penta-acetylated hv1) and used them to generate polyclonal antibodies specific for acetylated forms (mono-, di-, tri-, etc.) of these histones. Neither of these antisera recognizes histone that is unacetylated. Immunoblotting analyses demonstrate that both transcription-related and deposition-related acetate groups on H4 are recognized by both antisera. In addition, the antiserum raised against penta-acetylated hv1 also recognizes acetylated forms of this variant. Immunofluorescent analyses with both antisera demonstrate that, as expected, histone acetylation is specific to macronuclei (or new macronuclei) at all stages of the life cycle except when micronuclei undergo periods of rapid replication and chromatin assembly. During this time micronuclear staining is also detected. Our results also suggest that transcription-related acetylation begins selectively in new macronuclei immediately after the second postzygotic division. Acetylated histone is not observed in new micronuclei during stages corresponding to anlagen development and, therefore, histone acetylation can be distributed asymmetrically in development. Equally striking is the rapid turnover of acetylated histone in parental macronuclei during the time of their inactivation and elimination from the cell. Taken together, these data lend strong support to the idea that modulation of histone acetylation plays an important role in gene activation and in chromatin assembly.
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spelling pubmed-21155422008-05-01 Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena J Cell Biol Articles In this study, we have constructed synthetic peptides which are identical to hyperacetylated amino termini of two Tetrahymena core histones (tetra-acetylated H4 and penta-acetylated hv1) and used them to generate polyclonal antibodies specific for acetylated forms (mono-, di-, tri-, etc.) of these histones. Neither of these antisera recognizes histone that is unacetylated. Immunoblotting analyses demonstrate that both transcription-related and deposition-related acetate groups on H4 are recognized by both antisera. In addition, the antiserum raised against penta-acetylated hv1 also recognizes acetylated forms of this variant. Immunofluorescent analyses with both antisera demonstrate that, as expected, histone acetylation is specific to macronuclei (or new macronuclei) at all stages of the life cycle except when micronuclei undergo periods of rapid replication and chromatin assembly. During this time micronuclear staining is also detected. Our results also suggest that transcription-related acetylation begins selectively in new macronuclei immediately after the second postzygotic division. Acetylated histone is not observed in new micronuclei during stages corresponding to anlagen development and, therefore, histone acetylation can be distributed asymmetrically in development. Equally striking is the rapid turnover of acetylated histone in parental macronuclei during the time of their inactivation and elimination from the cell. Taken together, these data lend strong support to the idea that modulation of histone acetylation plays an important role in gene activation and in chromatin assembly. The Rockefeller University Press 1989-05-01 /pmc/articles/PMC2115542/ /pubmed/2654136 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena
title Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena
title_full Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena
title_fullStr Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena
title_full_unstemmed Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena
title_short Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena
title_sort antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in tetrahymena
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115542/
https://www.ncbi.nlm.nih.gov/pubmed/2654136