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Concerted action of Aurora B, Polo and NHK-1 kinases in centromere-specific histone 2A phosphorylation.

Brittle AL, Nanba Y, Ito T, Ohkura H - Exp. Cell Res. (2007)

Bottom Line: We found that the Aurora B kinase complex is essential for this phosphorylation at centromeres, while Polo kinase is required to down-regulate H2A phosphorylation on chromosome arms in mitosis.Epistasis analysis indicated that Polo functions upstream of the H2A kinase NHK-1 but parallel to Aurora B.Therefore, multiple mitotic kinases work together to specify the spatial and temporal pattern of H2A T119 phosphorylation.

View Article: PubMed Central - PubMed

Affiliation: The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, School of Biological Sciences, The University of Edinburgh, Edinburgh, UK.

ABSTRACT
The spatial and temporal control of histone modifications is crucial for precise regulation of chromatin structure and function. Here we report that phosphorylation of H2A at threonine 119 (T119) is enriched at centromere regions in Drosophila mitosis. We found that the Aurora B kinase complex is essential for this phosphorylation at centromeres, while Polo kinase is required to down-regulate H2A phosphorylation on chromosome arms in mitosis. Cyclin B degradation triggers loss of centromeric H2A phosphorylation at anaphase onset. Epistasis analysis indicated that Polo functions upstream of the H2A kinase NHK-1 but parallel to Aurora B. Therefore, multiple mitotic kinases work together to specify the spatial and temporal pattern of H2A T119 phosphorylation.

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Dynamic change of H2A T119 phosphorylation in the cell cycle. S2 cells were immunostained with anti-dH2A-pT119 antibody. H2A T119 phosphorylation was over all chromatin in interphase (A) but enriched to centromeric regions in prophase (B) and maintained through prometaphase (C) and metaphase (E). The phosphorylation was lost in anaphase (F). The boxed region in C is magnified in D. Scale bar = 10 μm.
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fig1: Dynamic change of H2A T119 phosphorylation in the cell cycle. S2 cells were immunostained with anti-dH2A-pT119 antibody. H2A T119 phosphorylation was over all chromatin in interphase (A) but enriched to centromeric regions in prophase (B) and maintained through prometaphase (C) and metaphase (E). The phosphorylation was lost in anaphase (F). The boxed region in C is magnified in D. Scale bar = 10 μm.

Mentions: To examine the spatial and temporal control of H2A T119 phosphorylation in cells, we immunostained Drosophila S2 cells using an antibody which specifically recognises this phosphorylated form of H2A (anti-dH2A-pT119 [5]). We found a dynamic change in the phosphorylation pattern of H2A during the cell cycle. In interphase, phosphorylation was present throughout the chromatin in the nucleus (Fig. 1A). Interestingly, in mitosis, as the chromosomes begin to condense, phosphorylation was no longer spread throughout the chromatin but produced a more punctate pattern (Fig. 1B). Co-staining with a centromeric marker CID (the CENP-A homologue; [8,16]) revealed that in prometaphase and metaphase, phosphorylation was enriched in regions between and surrounding CENP-A positive regions, which we refer to as the centromeric regions (Figs. 1C–E). This phosphorylation became dramatically reduced at the onset of anaphase (Fig. 1F). Phosphorylation only returned on decondensed chromatin at the end of mitosis.


Concerted action of Aurora B, Polo and NHK-1 kinases in centromere-specific histone 2A phosphorylation.

Brittle AL, Nanba Y, Ito T, Ohkura H - Exp. Cell Res. (2007)

Dynamic change of H2A T119 phosphorylation in the cell cycle. S2 cells were immunostained with anti-dH2A-pT119 antibody. H2A T119 phosphorylation was over all chromatin in interphase (A) but enriched to centromeric regions in prophase (B) and maintained through prometaphase (C) and metaphase (E). The phosphorylation was lost in anaphase (F). The boxed region in C is magnified in D. Scale bar = 10 μm.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2131725&req=5

fig1: Dynamic change of H2A T119 phosphorylation in the cell cycle. S2 cells were immunostained with anti-dH2A-pT119 antibody. H2A T119 phosphorylation was over all chromatin in interphase (A) but enriched to centromeric regions in prophase (B) and maintained through prometaphase (C) and metaphase (E). The phosphorylation was lost in anaphase (F). The boxed region in C is magnified in D. Scale bar = 10 μm.
Mentions: To examine the spatial and temporal control of H2A T119 phosphorylation in cells, we immunostained Drosophila S2 cells using an antibody which specifically recognises this phosphorylated form of H2A (anti-dH2A-pT119 [5]). We found a dynamic change in the phosphorylation pattern of H2A during the cell cycle. In interphase, phosphorylation was present throughout the chromatin in the nucleus (Fig. 1A). Interestingly, in mitosis, as the chromosomes begin to condense, phosphorylation was no longer spread throughout the chromatin but produced a more punctate pattern (Fig. 1B). Co-staining with a centromeric marker CID (the CENP-A homologue; [8,16]) revealed that in prometaphase and metaphase, phosphorylation was enriched in regions between and surrounding CENP-A positive regions, which we refer to as the centromeric regions (Figs. 1C–E). This phosphorylation became dramatically reduced at the onset of anaphase (Fig. 1F). Phosphorylation only returned on decondensed chromatin at the end of mitosis.

Bottom Line: We found that the Aurora B kinase complex is essential for this phosphorylation at centromeres, while Polo kinase is required to down-regulate H2A phosphorylation on chromosome arms in mitosis.Epistasis analysis indicated that Polo functions upstream of the H2A kinase NHK-1 but parallel to Aurora B.Therefore, multiple mitotic kinases work together to specify the spatial and temporal pattern of H2A T119 phosphorylation.

View Article: PubMed Central - PubMed

Affiliation: The Wellcome Trust Centre for Cell Biology and Institute of Cell Biology, School of Biological Sciences, The University of Edinburgh, Edinburgh, UK.

ABSTRACT
The spatial and temporal control of histone modifications is crucial for precise regulation of chromatin structure and function. Here we report that phosphorylation of H2A at threonine 119 (T119) is enriched at centromere regions in Drosophila mitosis. We found that the Aurora B kinase complex is essential for this phosphorylation at centromeres, while Polo kinase is required to down-regulate H2A phosphorylation on chromosome arms in mitosis. Cyclin B degradation triggers loss of centromeric H2A phosphorylation at anaphase onset. Epistasis analysis indicated that Polo functions upstream of the H2A kinase NHK-1 but parallel to Aurora B. Therefore, multiple mitotic kinases work together to specify the spatial and temporal pattern of H2A T119 phosphorylation.

Show MeSH