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Molecular and Cellular Biology, May 2007, p. 3589-3600, Vol. 27, No. 10
0270-7306/07/$08.00+0     doi:10.1128/MCB.02077-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Contribution of the Serine 129 of Histone H2A to Chromatin Structure{triangledown}

Michel Fink, Daniela Imholz, and Fritz Thoma*

Institute of Cell Biology, ETH Zurich, 8093 Zurich, Switzerland

Received 7 November 2006/ Returned for modification 19 December 2006/ Accepted 6 March 2007

Phosphorylation of a yeast histone H2A at C-terminal serine 129 has a central role in double-strand break repair. Mimicking H2A phosphorylation by replacement of serine 129 with glutamic acid (hta1-S129E) suggested that phosphorylation destabilizes chromatin structures and thereby facilitates the access of repair proteins. Here we have tested chromatin structures in hta1-S129 mutants and in a C-terminal tail deletion strain. We show that hta1-S129E affects neither nucleosome positioning in minichromosomes and genomic loci nor supercoiling of minichromosomes. Moreover, hta1-S129E has no effect on chromatin stability measured by conventional nuclease digestion, nor does it affect DNA accessibility and repair of UV-induced DNA lesions by nucleotide excision repair and photolyase in vivo. Similarly, deletion of the C-terminal tail has no effect on nucleosome positioning and stability. These data argue against a general role for the C-terminal tail in chromatin organization and suggest that phosphorylated H2A, {gamma}-H2AX in higher eukaryotes, acts by recruitment of repair components rather than by destabilizing chromatin structures.

* Corresponding author. Mailing address: Institute of Cell Biology, ETH Zurich, Schafmattstrasse 18, 8093 Zurich, Switzerland. Phone: 41 44 633 33 23. Fax: 41 44 633 10 69. E-mail: fritz.thoma{at}cell.biol.ethz.ch

{triangledown} Published ahead of print on 12 March 2007.

Molecular and Cellular Biology, May 2007, p. 3589-3600, Vol. 27, No. 10
0270-7306/07/$08.00+0     doi:10.1128/MCB.02077-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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