Centromere-specific acetylation of histone H4 in barley detected through three-dimensional microscopy

Centromere-specific acetylation of histone H4 in barley detected through three-dimensional... Histone acetylation affects chromatin conformation and transcriptional activity. However, the structural role of histone acetylation at specific chromosomal regions, such as the centromere, is poorly understood. In this study, histone H4 acetylation and its localization in barley interphase nuclei are revealed by three-dimensional microscopy. The centromeres form a ring-like allocation near the nuclear membrane in barley. Immunofluorescence studies on non-fixed, interphase nuclei treatment revealed ring-like distribution of the highly acetylated histone H4, located near the nuclear membrane at one pole of the nucleus. This fluorescent structure was similar to the centromere cluster and referred to as hyperacetylated region (HAR). The distribution pattern of the acetylated histone H4 was similar to each of the K5, K8, K12 and K16 lysine residues, although H4 acetylated at K5, K8 and K12 residues was found in almost all nuclei, whereas H4 acetylated at K16 was weakly observed in only half of the nuclei. Each HAR consists of two strongly acetylated cores and a halo-like, less acetylated surrounding area. Fluorescence signals from centromere-specific repetitive sequences of barley, detected through three-dimensional fluorescence in situ hybridization (3D-FISH), co-localized with the HAR corresponding to the K5 residue acetylation, but the signals did not completely overlap each other. These findings indicate that histone acetylation specifically occurring at the centromeres likely have certain structural roles for the centromere. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Centromere-specific acetylation of histone H4 in barley detected through three-dimensional microscopy

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Publisher
Springer Journals
Copyright
Copyright © 2003 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1022375017938
Publisher site
See Article on Publisher Site

Abstract

Histone acetylation affects chromatin conformation and transcriptional activity. However, the structural role of histone acetylation at specific chromosomal regions, such as the centromere, is poorly understood. In this study, histone H4 acetylation and its localization in barley interphase nuclei are revealed by three-dimensional microscopy. The centromeres form a ring-like allocation near the nuclear membrane in barley. Immunofluorescence studies on non-fixed, interphase nuclei treatment revealed ring-like distribution of the highly acetylated histone H4, located near the nuclear membrane at one pole of the nucleus. This fluorescent structure was similar to the centromere cluster and referred to as hyperacetylated region (HAR). The distribution pattern of the acetylated histone H4 was similar to each of the K5, K8, K12 and K16 lysine residues, although H4 acetylated at K5, K8 and K12 residues was found in almost all nuclei, whereas H4 acetylated at K16 was weakly observed in only half of the nuclei. Each HAR consists of two strongly acetylated cores and a halo-like, less acetylated surrounding area. Fluorescence signals from centromere-specific repetitive sequences of barley, detected through three-dimensional fluorescence in situ hybridization (3D-FISH), co-localized with the HAR corresponding to the K5 residue acetylation, but the signals did not completely overlap each other. These findings indicate that histone acetylation specifically occurring at the centromeres likely have certain structural roles for the centromere.

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 7, 2004

References

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