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Volume 272, Number 2, Issue of January 10, 1997 pp. 916-923
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Phosphorylation of Linker Histones by a Protein Kinase A-like Activity in Mitotic Nuclei

(Received for publication, September 12, 1996)

Melody T. Sweet Dagger , Gail Carlson § , Richard G. Cook par , David Nelson § and C. David Allis **

From the Dagger  Department of Biology, Syracuse University, Syracuse, New York 13244, the § Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, the par  Department of Microbiology and Immunology, Baylor College of Medicine, Houston, Texas 77030, and the ** Department of Biology, University of Rochester, Rochester, New York 14627

Micronuclear linker histones of the ciliated protozoan, Tetrahymena thermophila, are extensively phosphorylated in vivo. Each of these polypeptides, alpha , beta , gamma , and delta , contains sites for phosphorylation by cyclic-AMP dependent protein kinase (PKA) but not Cdc2 kinase, and some data have been presented implicating PKA kinase in their phosphorylation in vitro and in vivo (Sweet, M. T., and Allis, C. D. (1993) Chromosoma 102, 637-647; Sweet, M. T., Jones, K., and Allis, C. D. (1996) J. Cell Biol., in press). In this report we have extended these analyses by showing that Cdc2 and PKA kinase are not evenly distributed between micro- and macronuclei. Macronuclei, but not micronuclei, contain a 36-kDa polypeptide that is immunoreactive with p34Cdc2 antibodies. In contrast, a 40-kDa polypeptide is detected with PKA antibodies in micronuclei, that is not detected in macronuclei. In support, extracts from micronuclei, but not macronuclei, contain a kinase activity that resembles some, but not all, characteristics of PKA from other sources. Immunodepletion experiments using anti-PKA antibodies show that a 40-kDa polypeptide can be specifically removed from these extracts with a concomitant loss in kinase activity. Microsequence analyses of delta  demonstrate that this linker histone is phosphorylated in vivo on two PKA consensus sequences located in its carboxyl-terminal domain, an optimum PKA consensus sequence, Arg-Lys-Asn-<UNL>Ser</UNL>, and a less optimal PKA sequence, Lys-Ser-<UNL>Ser</UNL>-Val. Collectively, these results suggest that PKA or a PKA-like kinase is responsible for the phosphorylation of linker histone in mitotically dividing micronuclei. In contrast, macronuclei, which divide amitotically, phosphorylate linker histone H1 using a distinct, Cdc2-like kinase.


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