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J Biol Chem, Vol. 274, Issue 21, 14533-14536, May 21, 1999

COMMUNICATION
Identification and Mutation of Phosphorylation Sites in a Linker Histone
PHOSPHORYLATION OF MACRONUCLEAR H1 IS NOT ESSENTIAL FOR VIABILITY IN TETRAHYMENA

Craig A. Mizzen, Yali Dou^§, Yugang Liu^§, Richard G. Cook^¶, Martin A. Gorovsky^§, and C. David Allis

From the  Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908, the ^§ Department of Biology, University of Rochester, Rochester, New York 14627, and the ^¶ Department of Microbiology and Immunology, Baylor College of Medicine, Houston, Texas 77030

Linker histone phosphorylation has been suggested to play roles in both chromosome condensation and transcriptional regulation. In the ciliated protozoan Tetrahymena, in contrast to many eukaryotes, histone H1 of macronuclei is highly phosphorylated during interphase. Macronuclei divide amitotically without overt chromosome condensation in this organism, suggesting that requirements for phosphorylation of macronuclear H1 may be limited to transcriptional regulation. Here we report the major sites of phosphorylation of macronuclear H1 in Tetrahymena thermophila. Five phosphorylation sites, present in a single cluster, were identified by sequencing ³²P-labeled peptides isolated from tryptic peptide maps. Phosphothreonine was detected within two TPVK motifs and one TPTK motif that resemble established p34^cdc2 kinase consensus sequences. Phosphoserine was detected at two non-proline-directed sites that do not resemble known kinase consensus sequences. Phosphorylation at the two noncanonical sites appears to be hierarchical because it was observed only when a nearby p34^cdc2 site was also phosphorylated. Cells expressing macronuclear H1 containing alanine substitutions at all five of these phosphorylation sites were viable even though macronuclear H1 phosphorylation was abolished. These data suggest that the five sites identified comprise the entire collection of sites utilized by Tetrahymena and demonstrate that phosphorylation of macronuclear H1, like the protein itself, is not essential for viability in Tetrahymena.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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