First published online January 19, 2005; 10.1105/tpc.104.028522
The Plant Cell 17:572-583 (2005)
© 2005 American Society of Plant Biologists
Phosphoserines on Maize CENTROMERIC HISTONE H3 and Histone H3 Demarcate the Centromere and Pericentromere during Chromosome Segregation
Xiaolan Zhanga,1,
Xuexian Lia,1,
Joshua B. Marshalla,
Cathy X. Zhonga and
R. Kelly Dawea,b,2
a Department of Plant Biology, University of Georgia, Athens, Georgia 30602
b Department of Genetics, University of Georgia, Athens, Georgia 30602
2 To whom correspondence should be addressed. E-mail kelly{at}plantbio.uga.edu; fax 706-542-1805.
We have identified and characterized a 17- to 18-kD Ser50-phosphorylated form of maize (Zea mays) CENTROMERIC HISTONE H3 (phCENH3-Ser50). Immunostaining in both mitosis and meiosis indicates that CENH3-Ser50 phosphorylation begins in prophase/diplotene, increases to a maximum at prometaphase-metaphase, and drops during anaphase. Dephosphorylation is precipitous (approximately sixfold) at the metaphase–anaphase transition, suggesting a role in the spindle checkpoint. Although phCENH3-Ser50 lies within a region that lacks homology to any other known histone, its closest counterpart is the phospho-Ser28 residue of histone H3 (phH3-Ser28). CENH3-Ser50 and H3-Ser28 are phosphorylated with nearly identical kinetics, but the former is restricted to centromeres and the latter to pericentromeres. Opposing centromeres separate in prometaphase, whereas the phH3-Ser28–marked pericentromeres remain attached and coalesce into a well-defined tether that binds the centromeres together. We propose that a centromere-initiated wave of histone phosphorylation is an early step in defining the two major structural domains required for chromosome segregation: centromere (alignment, motility) and pericentromere (cohesion).
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