Comprehensive analysis of dynamics of histone H4 acetylation in mitotic barley [Hordeum vulgare] cells

Nucleosomal histones are covalently modified at specific amino acid residues. In the case of histone H4, four lysines (K5, K8, K12, and K16) are acetylated. In the current studies, we examined the dynamics of histone H4 acetylation at K8 and K12 in mitotic barley cells using a three-dimensional immu...

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Published inGenes & Genetic Systems Vol. 80; no. 4; pp. 269 - 276
Main Authors Wako, T.(National Inst. of Agrobiological Sciences, Tsukuba, Ibaraki (Japan)), Murakami, Y, Fukui, K
Format Journal Article
LanguageEnglish
Published Japan The Genetics Society of Japan 2005
Japan Science and Technology Agency
Subjects
ACETILACION
ACETYLATION
barley
Centromere - metabolism
CHROMOSOME
CHROMOSOMES
Chromosomes, Plant - metabolism
CITOGENETICA
CROMOSOMAS
CYTOGENETICS
CYTOGENETIQUE
HISTONAS
HISTONE
histone H4 acetylation
HISTONES
Histones - metabolism
Hordeum - cytology
Hordeum - physiology
HORDEUM VULGARE
Lysine - metabolism
MITOSE
MITOSIS
mitotic chromosome
nucleolar organizing region (NOR)
Nucleolus Organizer Region - metabolism
Nucleosomes - metabolism
Prophase - physiology
Protein Processing, Post-Translational - physiology
Telophase - physiology
Online AccessGet full text
ISSN1341-7568
1880-5779
DOI10.1266/ggs.80.269

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Abstract Nucleosomal histones are covalently modified at specific amino acid residues. In the case of histone H4, four lysines (K5, K8, K12, and K16) are acetylated. In the current studies, we examined the dynamics of histone H4 acetylation at K8 and K12 in mitotic barley cells using a three-dimensional immunofluorescent method. Based on the results and previous studies on the dynamics of K5 and K16 acetylation, we provide a comprehensive view of the dynamics of H4 acetylation. Interphase nuclei exhibit strong acetylation in the centromeric region at K5, K8 and K12. In the case of K12, strong acetylation at nucleolar organizing regions was observed from prophase to anaphase. The dynamics of K12 were closely related to those of K5. On the other hand, K8 exhibited a pattern of almost uniform acetylation from prophase to telophase and strong acetylation in distal regions of chromosomes at both metaphase and anaphase, which is very similar to the dynamics of K16 acetylation. Thus, it appears that there is pair-wise acetylation of K12 and K5 in the nucleolar organizing regions and of K8 and K16 in the gene-rich regions. Together, these results suggest that pair-wise dynamics of H4 acetylation regulate chromosomal structure and function during the cell cycle.
AbstractList Nucleosomal histones are covalently modified at specific amino acid residues. In the case of histone H4, four lysines (K5, K8, K12, and K16) are acetylated. In the current studies, we examined the dynamics of histone H4 acetylation at K8 and K12 in mitotic barley cells using a three-dimensional immunofluorescent method. Based on the results and previous studies on the dynamics of K5 and K16 acetylation, we provide a comprehensive view of the dynamics of H4 acetylation. Interphase nuclei exhibit strong acetylation in the centromeric region at K5, K8 and K12. In the case of K12, strong acetylation at nucleolar organizing regions was observed from prophase to anaphase. The dynamics of K12 were closely related to those of K5. On the other hand, K8 exhibited a pattern of almost uniform acetylation from prophase to telophase and strong acetylation in distal regions of chromosomes at both metaphase and anaphase, which is very similar to the dynamics of K16 acetylation. Thus, it appears that there is pair-wise acetylation of K12 and K5 in the nucleolar organizing regions and of K8 and K16 in the gene-rich regions. Together, these results suggest that pair-wise dynamics of H4 acetylation regulate chromosomal structure and function during the cell cycle. INTRODUCTION Higher-order chromatin structure consists of nucleosomes, which are fundamental units made up of DNA and a histone octamer (two heterodimers of H2A/H2B and a tetramer of H3/H4). Each histone has a protruding N-terminal tail that is subject to various post-translational modifications, including acetylation, phosphorylation, and methylation, at specific amino acid residues. Histone acetylation is a well-documented modification that occurs at N-terminal lysine residues of core histones and plays an important role in various cellular functions (Spencer and Davie, 1999, Strahl and Allis, 2000). Histone acetylation participates in transcription activation and is regulated by histone acetyltransferases (HATs), which are subunits of transcription factors (Marmorstein and Roth, 2001). The reverse reaction, histone deacetylation, leads to transcription silencing and is mediated by histone deacetylases (HDACs), which are found in transcription repressors (Marks et al., 2004). Specific acetylation occurs on the newly synthesized histones in the cyloplasm (Sobel et al., 1995) and is required for DNA double-strand break repair (Bird et al., 2002). Replication-related histone acetylation is also reported in flow-sorted nuclei from field bean, barley, and Arabidopsis (Jasencakova et al., 2000, 2001, 2003). Distinct combinations of covalent modifications of histone tails are thought to work as epigenetic code, referred to as a “histone code”. These combinations of modifications regulate the interactions of histones with DNA strands, chromatin-associated proteins, or protein complexes, which, in turn, control chromatin function (Strahl and Allis, 2000, Jenuwein and Allis, 2001). For example, there is evidence that methylation of histone H3 works in concert with other modifications to mediate transcription silencing (Jenuwein and Allis, 2001).
Nucleosomal histones are covalently modified at specific amino acid residues. In the case of histone H4, four lysines (K5, K8, K12, and K16) are acetylated. In the current studies, we examined the dynamics of histone H4 acetylation at K8 and K12 in mitotic barley cells using a three-dimensional immunofluorescent method. Based on the results and previous studies on the dynamics of K5 and K16 acetylation, we provide a comprehensive view of the dynamics of H4 acetylation. Interphase nuclei exhibit strong acetylation in the centromeric region at K5, K8 and K12. In the case of K12, strong acetylation at nucleolar organizing regions was observed from prophase to anaphase. The dynamics of K12 were closely related to those of K5. On the other hand, K8 exhibited a pattern of almost uniform acetylation from prophase to telophase and strong acetylation in distal regions of chromosomes at both metaphase and anaphase, which is very similar to the dynamics of K16 acetylation. Thus, it appears that there is pair-wise acetylation of K12 and K5 in the nucleolar organizing regions and of K8 and K16 in the gene-rich regions. Together, these results suggest that pair-wise dynamics of H4 acetylation regulate chromosomal structure and function during the cell cycle.
Nucleosomal histones are covalently modified at specific amino acid residues. In the case of histone H4, four lysines (K5, K8, K12, and K16) are acetylated. In the current studies, we examined the dynamics of histone H4 acetylation at K8 and K12 in mitotic barley cells using a three-dimensional immunofluorescent method. Based on the results and previous studies on the dynamics of K5 and K16 acetylation, we provide a comprehensive view of the dynamics of H4 acetylation. Interphase nuclei exhibit strong acetylation in the centromeric region at K5, K8 and K12. In the case of K12, strong acetylation at nucleolar organizing regions was observed from prophase to anaphase. The dynamics of K12 were closely related to those of K5. On the other hand, K8 exhibited a pattern of almost uniform acetylation from prophase to telophase and strong acetylation in distal regions of chromosomes at both metaphase and anaphase, which is very similar to the dynamics of K16 acetylation. Thus, it appears that there is pair-wise acetylation of K12 and K5 in the nucleolar organizing regions and of K8 and K16 in the gene-rich regions. Together, these results suggest that pair-wise dynamics of H4 acetylation regulate chromosomal structure and function during the cell cycle.Nucleosomal histones are covalently modified at specific amino acid residues. In the case of histone H4, four lysines (K5, K8, K12, and K16) are acetylated. In the current studies, we examined the dynamics of histone H4 acetylation at K8 and K12 in mitotic barley cells using a three-dimensional immunofluorescent method. Based on the results and previous studies on the dynamics of K5 and K16 acetylation, we provide a comprehensive view of the dynamics of H4 acetylation. Interphase nuclei exhibit strong acetylation in the centromeric region at K5, K8 and K12. In the case of K12, strong acetylation at nucleolar organizing regions was observed from prophase to anaphase. The dynamics of K12 were closely related to those of K5. On the other hand, K8 exhibited a pattern of almost uniform acetylation from prophase to telophase and strong acetylation in distal regions of chromosomes at both metaphase and anaphase, which is very similar to the dynamics of K16 acetylation. Thus, it appears that there is pair-wise acetylation of K12 and K5 in the nucleolar organizing regions and of K8 and K16 in the gene-rich regions. Together, these results suggest that pair-wise dynamics of H4 acetylation regulate chromosomal structure and function during the cell cycle.
Author Fukui, K
Wako, T.(National Inst. of Agrobiological Sciences, Tsukuba, Ibaraki (Japan))
Murakami, Y
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Snippet Nucleosomal histones are covalently modified at specific amino acid residues. In the case of histone H4, four lysines (K5, K8, K12, and K16) are acetylated. In...
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SubjectTerms ACETILACION
ACETYLATION
barley
Centromere - metabolism
CHROMOSOME
CHROMOSOMES
Chromosomes, Plant - metabolism
CITOGENETICA
CROMOSOMAS
CYTOGENETICS
CYTOGENETIQUE
HISTONAS
HISTONE
histone H4 acetylation
HISTONES
Histones - metabolism
Hordeum - cytology
Hordeum - physiology
HORDEUM VULGARE
Lysine - metabolism
MITOSE
MITOSIS
mitotic chromosome
nucleolar organizing region (NOR)
Nucleolus Organizer Region - metabolism
Nucleosomes - metabolism
Prophase - physiology
Protein Processing, Post-Translational - physiology
Telophase - physiology
Title Comprehensive analysis of dynamics of histone H4 acetylation in mitotic barley [Hordeum vulgare] cells
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