Kinetic analysis of histone acetylation turnover and trichostatin A induced hyper- and hypoacetylation in alfalfa
Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase, and steady-state acetylation labeling. Acetylation turnover half-lives of about 0.5 h were obs...
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Published in | Biochemistry and cell biology Vol. 80; no. 3; pp. 279 - 293 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Ottawa, Canada
NRC Research Press
2002
Canadian Science Publishing NRC Research Press |
Subjects | |
Online Access | Get full text |
ISSN | 0829-8211 1208-6002 |
DOI | 10.1139/o02-021 |
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Abstract | Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase, and steady-state acetylation labeling. Acetylation turnover half-lives of about 0.5 h were observed by all methods used for histones H3, H4, and H2B. This is consistent with the rate at which changes in gene expression occur in plants. Treatment with histone deacetylase inhibitor Trichostatin A (TSA) induced hyperacetylation at a similar rate. Replacement histone variant H3.2, preferentially localized in highly acetylated chromatin, displayed faster acetyl turnover. Histone H2A with a low level of acetylation was not subject to rapid turnover or hyperacetylation. Patterns of acetate labeling revealed fundamental differences between histone H3 versus histones H4 and H2B. In H3, acetylation of all molecules, limited by lysine methylation, had similar rates, independent of the level of lysine acetylation. Acetylation of histones H4 and H2B was seen in only a fraction of all molecules and involved multiacetylation. Acetylation turnover rates increased from mono- to penta- and hexaacetylated forms, respectively. TSA was an effective inhibitor of alfalfa histone deacetylases in vivo and caused a doubling in steady-state acetylation levels by 46 h after addition. However, hyperacetylation was transient due to loss of TSA inhibition. TSA-induced overexpression of cellular deacetylase activity produced hypoacetylation by 18 h treatment with enhanced acetate turnover labeling of alfalfa histones. Thus, application of TSA to change gene expression in vivo in plants may have unexpected consequences. |
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AbstractList | Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase and steady-state acetylation labeling. Application of Trichostatin A to change gene expression in vivo in plants may have unexpected consequences. Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase, and steady-state acetylation labeling. Acetylation turnover half-lives of about 0.5 h were observed by all methods used for histones H3, H4, and H2B. This is consistent with the rate at which changes in gene expression occur in plants. Treatment with histone deacetylase inhibitor Trichostatin A (TSA) induced hyperacetylation at a similar rate. Replacement histone variant H3.2, preferentially localized in highly acetylated chromatin, displayed faster acetyl turnover. Histone H2A with a low level of acetylation was not subject to rapid turnover or hyperacetylation. Patterns of acetate labeling revealed fundamental differences between histone H3 versus histones H4 and H2B. In H3, acetylation of all molecules, limited by lysine methylation, had similar rates, independent of the level of lysine acetylation. Acetylation of histones H4 and H2B was seen in only a fraction of all molecules and involved multiacetylation. Acetylation turnover rates increased from mono- to penta- and hexaacetylated forms, respectively. TSA was an effective inhibitor of alfalfa histone deacetylases in vivo and caused a doubling in steady-state acetylation levels by 4-6 h after addition. However, hyperacetylation was transient due to loss of TSA inhibition. TSA-induced overexpression of cellular deacetylase activity produced hypoacetylation by 18 h treatment with enhanced acetate turnover labeling of alfalfa histones. Thus, application of TSA to change gene expression in vivo in plants may have unexpected consequences. Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase, and steady-state acetylation labeling. Acetylation turnover half-lives of about 0.5 h were observed by all methods used for histones H3, H4, and H2B. This is consistent with the rate at which changes in gene expression occur in plants. Treatment with histone deacetylase inhibitor Trichostatin A (TSA) induced hyperacetylation at a similar rate. Replacement histone variant H3.2, preferentially localized in highly acetylated chromatin, displayed faster acetyl turnover. Histone H2A with a low level of acetylation was not subject to rapid turnover or hyperacetylation. Patterns of acetate labeling revealed fundamental differences between histone H3 versus histones H4 and H2B. In H3, acetylation of all molecules, limited by lysine methylation, had similar rates, independent of the level of lysine acetylation. Acetylation of histones H4 and H2B was seen in only a fraction of all molecules and involved multiacetylation. Acetylation turnover rates increased from mono- to penta- and hexaacetylated forms, respectively. TSA was an effective inhibitor of alfalfa histone deacetylases in vivo and caused a doubling in steady-state acetylation levels by 46 h after addition. However, hyperacetylation was transient due to loss of TSA inhibition. TSA-induced overexpression of cellular deacetylase activity produced hypoacetylation by 18 h treatment with enhanced acetate turnover labeling of alfalfa histones. Thus, application of TSA to change gene expression in vivo in plants may have unexpected consequences. Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase, and steady-state acetylation labeling. Acetylation turnover half-lives of about 0.5 h were observed by all methods used for histones H3, H4, and H2B. This is consistent with the rate at which changes in gene expression occur in plants. Treatment with histone deacetylase inhibitor Trichostatin A (TSA) induced hyperacetylation at a similar rate. Replacement histone variant H3.2, preferentially localized in highly acetylated chromatin, displayed faster acetyl turnover. Histone H2A with a low level of acetylation was not subject to rapid turnover or hyperacetylation. Patterns of acetate labeling revealed fundamental differences between histone H3 versus histones H4 and H2B. In H3, acetylation of all molecules, limited by lysine methylation, had similar rates, independent of the level of lysine acetylation. Acetylation of histones H4 and H2B was seen in only a fraction of all molecules and involved multiacetylation. Acetylation turnover rates increased from mono- to penta- and hexaacetylated forms, respectively. TSA was an effective inhibitor of alfalfa histone deacetylases in vivo and caused a doubling in steady-state acetylation levels by 4-6 h after addition. However, hyperacetylation was transient due to loss of TSA inhibition. TSA-induced overexpression of cellular deacetylase activity produced hypoacetylation by 18 h treatment with enhanced acetate turnover labeling of alfalfa histones. Thus, application of TSA to change gene expression in vivo in plants may have unexpected consequences.Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase, and steady-state acetylation labeling. Acetylation turnover half-lives of about 0.5 h were observed by all methods used for histones H3, H4, and H2B. This is consistent with the rate at which changes in gene expression occur in plants. Treatment with histone deacetylase inhibitor Trichostatin A (TSA) induced hyperacetylation at a similar rate. Replacement histone variant H3.2, preferentially localized in highly acetylated chromatin, displayed faster acetyl turnover. Histone H2A with a low level of acetylation was not subject to rapid turnover or hyperacetylation. Patterns of acetate labeling revealed fundamental differences between histone H3 versus histones H4 and H2B. In H3, acetylation of all molecules, limited by lysine methylation, had similar rates, independent of the level of lysine acetylation. Acetylation of histones H4 and H2B was seen in only a fraction of all molecules and involved multiacetylation. Acetylation turnover rates increased from mono- to penta- and hexaacetylated forms, respectively. TSA was an effective inhibitor of alfalfa histone deacetylases in vivo and caused a doubling in steady-state acetylation levels by 4-6 h after addition. However, hyperacetylation was transient due to loss of TSA inhibition. TSA-induced overexpression of cellular deacetylase activity produced hypoacetylation by 18 h treatment with enhanced acetate turnover labeling of alfalfa histones. Thus, application of TSA to change gene expression in vivo in plants may have unexpected consequences. |
Abstract_FL | L'acétylation dynamique des histones est une caractéristique de la transcription de la chromatine. Cet article présente les premières estimations du taux de renouvellement des groupes acétyle chez les plantes, obtenues en mesurant l'acétylation grâce à un marquage bref, suivi ou non d'une chasse, et à un marquage à l'équilibre de cellules de luzerne. La demi-vie de renouvellement des groupes acétyle des histones H3, H4 et H2B est environ 0,50 h selon toutes les méthodes. Cela concorde avec la vitesse de modification de l'expression des gènes chez les plantes. Une incubation en présence de Trichostatine A (TSA), un inhibiteur des histones désacétylases, induit une hyperacétylation à une vitesse similaire. Le taux de renouvellement des groupes acétyle de l'histone H3.2 de remplacement, qui se trouve préférentiellement dans la chromatine hyperacétylée, est plus rapide. L'histone H2A peu acétylée a un taux de renouvellement des groupes acétyle lent et elle n'est pas sujette à l'hyperacétylation. Le marquage avec l'acétate montre qu'il y a des différences fondamentales entre l'histone H3, d'une part, et les histones H4 et H2B, d'autre part. L'acétylation de toutes les molécules d'histone H3, limitée par la méthylation des résidus lysine, se fait à la même vitesse, indépendamment du niveau d'acétylation des résidus lysine. Par contre, seulement une fraction de toutes les molécules des histones H4 et H2B sont acétylées et cela fait intervenir de multiples acétylations. Les taux de renouvellement des groupes acétyle augmentent en allant des formes mono-acétylées aux formes penta- et hexa-acétylées. La TSA est un bon inhibiteur des histones désacétylases de la luzerne in vivo et le taux d'acétylation à l'équilibre double 4 à 6 h après traitement avec la TSA. Cependant, l'hyperacétylation est transitoire car l'inhibition par la TSA disparaît progressivement. La TSA induit la surexpression des désacétylases cellulaires, ce qui engendre une hypoacétylation, 18 h aprés traitement avec la TSA, et une augmentation du taux de renouvellement des groupes acétyle des histones de la luzerne. Donc, l'application de TSA à des plantes afin de modifier l'expression de leurs gènes in vivo pourrait avoir des conséquences imprévues.[Traduit par la Rédaction] |
Author | Kapros, T Waterborg, J.H |
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Snippet | Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported,... |
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SubjectTerms | Acetates Acetates - metabolism Acetylation Alfalfa Cells Cellular biology Chromatin Enzyme Inhibitors Enzyme Inhibitors - pharmacology Flowers & plants Genetics Histone Deacetylase Inhibitors Histone Deacetylases Histone Deacetylases - metabolism Histones Histones - metabolism Hydroxamic Acids Hydroxamic Acids - pharmacology Kinetics Medicago sativa Medicago sativa - metabolism metabolism methods pharmacology plant biochemistry plant physiology Staining and Labeling Staining and Labeling - methods |
Title | Kinetic analysis of histone acetylation turnover and trichostatin A induced hyper- and hypoacetylation in alfalfa |
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