Identification and characterization of plant Haspin kinase as a histone H3 threonine kinase

<p>Abstract</p> <p>Background</p> <p>Haspin kinases are mitotic kinases that are well-conserved from yeast to human. Human Haspin is a histone H3 Thr3 kinase that has important roles in chromosome cohesion during mitosis. Moreover, phosphorylation of histone H3 at Thr3...

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Main Authors: Omura Tomohiro, Matsunaga Sachihiro, Kurihara Daisuke, Higashiyama Tetsuya, Fukui Kiichi
Format: Article
Language:English
Published: BMC 2011-04-01
Series:BMC Plant Biology
Online Access:http://www.biomedcentral.com/1471-2229/11/73
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spelling doaj-ce5909a41eb94027b7d23510505fff2b2020-11-24T21:44:28ZengBMCBMC Plant Biology1471-22292011-04-011117310.1186/1471-2229-11-73Identification and characterization of plant Haspin kinase as a histone H3 threonine kinaseOmura TomohiroMatsunaga SachihiroKurihara DaisukeHigashiyama TetsuyaFukui Kiichi<p>Abstract</p> <p>Background</p> <p>Haspin kinases are mitotic kinases that are well-conserved from yeast to human. Human Haspin is a histone H3 Thr3 kinase that has important roles in chromosome cohesion during mitosis. Moreover, phosphorylation of histone H3 at Thr3 by Haspin in fission yeast, <it>Xenopus</it>, and human is required for accumulation of Aurora B on the centromere, and the subsequent activation of Aurora B kinase activity for accurate chromosome alignment and segregation. Although extensive analyses of Haspin have been carried out in yeast and animals, the function of Haspin in organogenesis remains unclear.</p> <p>Results</p> <p>Here, we identified a Haspin kinase, designated AtHaspin, in <it>Arabidopsis thaliana</it>. The purified AtHaspin phosphorylated histone H3 at both Thr3 and Thr11 <it>in vitro</it>. Live imaging of AtHaspin-tdTomato and GFP-α-tubulin in BY-2 cells showed that AtHaspin-tdTomato localized on chromosomes during prometaphase and metaphase, and around the cell plate during cytokinesis. This localization of AtHaspin overlapped with that of phosphorylated Thr3 and Thr11 of histone H3 in BY-2 cells. AtHaspin-GFP driven by the native promoter was expressed in root meristems, shoot meristems, floral meristems, and throughout the whole embryo at stages of high cell division. Overexpression of a kinase domain mutant of AtHaspin decreased the size of the root meristem, which delayed root growth.</p> <p>Conclusions</p> <p>Our results indicated that the Haspin kinase is a histone H3 threonine kinase in <it>A. thaliana</it>. AtHaspin phosphorylated histone H3 at both Thr3 and Thr11 <it>in vitro</it>. The expression and dominant-negative analysis showed that AtHaspin may have a role in mitotic cell division during plant growth. Further analysis of coordinated mechanisms involving Haspin and Aurora kinases will shed new light on the regulation of chromosome segregation in cell division during plant growth and development.</p> http://www.biomedcentral.com/1471-2229/11/73
collection DOAJ
language English
format Article
sources DOAJ
author Omura Tomohiro
Matsunaga Sachihiro
Kurihara Daisuke
Higashiyama Tetsuya
Fukui Kiichi
spellingShingle Omura Tomohiro
Matsunaga Sachihiro
Kurihara Daisuke
Higashiyama Tetsuya
Fukui Kiichi
Identification and characterization of plant Haspin kinase as a histone H3 threonine kinase
BMC Plant Biology
author_facet Omura Tomohiro
Matsunaga Sachihiro
Kurihara Daisuke
Higashiyama Tetsuya
Fukui Kiichi
author_sort Omura Tomohiro
title Identification and characterization of plant Haspin kinase as a histone H3 threonine kinase
title_short Identification and characterization of plant Haspin kinase as a histone H3 threonine kinase
title_full Identification and characterization of plant Haspin kinase as a histone H3 threonine kinase
title_fullStr Identification and characterization of plant Haspin kinase as a histone H3 threonine kinase
title_full_unstemmed Identification and characterization of plant Haspin kinase as a histone H3 threonine kinase
title_sort identification and characterization of plant haspin kinase as a histone h3 threonine kinase
publisher BMC
series BMC Plant Biology
issn 1471-2229
publishDate 2011-04-01
description <p>Abstract</p> <p>Background</p> <p>Haspin kinases are mitotic kinases that are well-conserved from yeast to human. Human Haspin is a histone H3 Thr3 kinase that has important roles in chromosome cohesion during mitosis. Moreover, phosphorylation of histone H3 at Thr3 by Haspin in fission yeast, <it>Xenopus</it>, and human is required for accumulation of Aurora B on the centromere, and the subsequent activation of Aurora B kinase activity for accurate chromosome alignment and segregation. Although extensive analyses of Haspin have been carried out in yeast and animals, the function of Haspin in organogenesis remains unclear.</p> <p>Results</p> <p>Here, we identified a Haspin kinase, designated AtHaspin, in <it>Arabidopsis thaliana</it>. The purified AtHaspin phosphorylated histone H3 at both Thr3 and Thr11 <it>in vitro</it>. Live imaging of AtHaspin-tdTomato and GFP-α-tubulin in BY-2 cells showed that AtHaspin-tdTomato localized on chromosomes during prometaphase and metaphase, and around the cell plate during cytokinesis. This localization of AtHaspin overlapped with that of phosphorylated Thr3 and Thr11 of histone H3 in BY-2 cells. AtHaspin-GFP driven by the native promoter was expressed in root meristems, shoot meristems, floral meristems, and throughout the whole embryo at stages of high cell division. Overexpression of a kinase domain mutant of AtHaspin decreased the size of the root meristem, which delayed root growth.</p> <p>Conclusions</p> <p>Our results indicated that the Haspin kinase is a histone H3 threonine kinase in <it>A. thaliana</it>. AtHaspin phosphorylated histone H3 at both Thr3 and Thr11 <it>in vitro</it>. The expression and dominant-negative analysis showed that AtHaspin may have a role in mitotic cell division during plant growth. Further analysis of coordinated mechanisms involving Haspin and Aurora kinases will shed new light on the regulation of chromosome segregation in cell division during plant growth and development.</p>
url http://www.biomedcentral.com/1471-2229/11/73
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