Histones histone kinases

Arion, D., Meijer, L., Brizuela, L., and Beach, D. (1988). cdc2 is a component of the M phase specific histone HI kinase evidence for identity withMPF. Cell 55 371-378. Balakier, H and Czolowska, R. (1977). Cytoplasmic control of nuclear maturation of mouse oocytes. Exp. Cell Res. 110 466-469. 

Fulka, J., Jr., Jung, T., and Moor, R. M. (1992). The fall of biological maturation promoting factor (MPF) and histone HI kinase activity during anaphase and telophase in mouse oocytes. Mol. Reprod. Devel. 32 378-382. 

Labbe, J. C., Picard, A. Peaucellier, G., Cavadore, J. C., Nurse, P., and Doree, M. (1989b). Purification of MPF from starfish identification as the HI histone kinase p34cpossible mechanism for its periodic activation. Cell 57 253-263. 

Rime, H., and Ozon, R. (1990). Protein phosphatases are involved in the in vivo activation of the histone HI kinase in mouse oocytes. Dev. Biol. 141 115-122. 

FIG. 3. HistoneHl kinase activity and schematic representation of the morphology of one-cell mouse embryos (3A) and two-cell stage blastomeres (3B) bisected at the respective G2 phases. N ote that histone H1 kinase activity rises autonomously in anucleate halves of both embryos and blastomeres. However, the degree of the autonomous activation is lower than in theit nucleate counterparts. Activity detected in nucleate halves obtained during respective M phases was taken as 100%. Note that the nucleate halves obtained at theit respective G2 stages do not activate histone HI kinase to the levels observed in the halves obtained in the M phase, and that the mitotic disassembly of microtubules was observed only when the level of histone HI kinase was between 35% and 46% in anucleate halves. 

Ciemerych MA, Tarkowski AK, Kubiak JZ 1998 Autonomous activation of histone HI kinase, cortical activity and microtubule organization in one- and two-cell mouse embryos. Biol Cell 90 557-564... 

Nurse Work in starfish suggested that Cdk activity remained quite high, so that is the simplest model, and that is likely to be the case in fission yeast as well. We are cataloguing all the different components to see if we can work out the regulation of Cdk. It is consistent with but not yet proven that cdk regulation could regulate S phase between meiosis I and meiosis II. But I am worried about this mouse observation. Did you look at total HI histone kinase ... 

Ito T (2003) Nucleosome assembly and remodehng. Curr Top Microbiol Immunol 274 1-22 Ito T, Tyler JK, Kadonaga JT (1997) Chromatin assembly factors a dual function in nucleosome formation and mobilization Genes Cells 2(10) 593-600 Ivanovska I, Khandan T, Ito T, Orr-Weaver TL (2005) A histone code in meiosis the histone kinase, NHK-1, is required for proper chromosomal architecture in Drosophila oocytes. Genes Dev 19(21) 2571-2582... 

Histone kinases responsible for N-phosphorylation have been isolated from regenerating rat liver [109] and Walker-256 carcinosarcoma cells [110]. One kinase with a pH optimum of 9.5 phosphorylated His-18 and His-75 of H4, while the other with a pH optimum of 6.5 phosphorylated lysine of HI. The enzyme from regenerating rat liver phosphorylated H4 at 1-phosphoryl histidine, while the carcinosarcoma enzyme phosphorylated H4 His at the position 3 [111]. Both kinases were cAMP independent [110]. Matthews and colleagues purified a 32-kDa histidine H4 kinase from yeast, Saccharomyces cerevisiae [112,113]. The enzyme phosphorylated His-75 (1-phosphoryl histidine) in H4. His-18 of H4 and other histidines in other core histones were not phosphorylated by this kinase [112]. Protein phosphatases 1, 2A, and 2C could dephosphorylate His-75 of H4 [114]. Applying a gel kinase approach to detect mammalian H4 histidine kinases, Besant and Attwood detected four activities in the 34-41 kDa range with extracts from porcine thymus [115]. 

The temporal sequence of H3 and H4 methylation after synthesis has been examined in Ehrlich ascites tumor cells [144] and trout testis [149]. Methylation lagged histone synthesis, and the histone was methylated after being bound to DNA. H4 methylation follows the stepwise acetylations and deacetylations [149]. It was suggested that methylation was involved in final arrangement of H3 and H4 on newly replicated DNA [144] and might be involved in histone interactions with other proteins such as histone kinases [149]. 

HISTIDINOL-PHOSPHATE PHOSPHATASE HISTIDYL-tRNA SYNTHETASE HISTONE KINASE Hofmann rule,... 

Lo, W.-S., Duggan, L., Tolga Emre, N.C., Belotserkovskya, R., Lane, W.S., Shiekhattar, R., and Berger, S.L., 2001, Snfl - a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science 293 1142-1146. 

A cyclic AMP independent protein kinase which catalyzes the phosphorylation of histidine in histones has been found in nuclei from rat tissue and in Walker-256 carcinosarcoma cell nuclei (96). Two histone kinases (ATP histone N-phosphotransferase) have been partially purified from the nuclei of the carcinosarcoma cells (78a). One of these enzymes preferentially phosphorylates histone H4 (IV, F2al) at an optimum pH of 9.5, while the other preferentially phosphorylates histone I (FI) at an optimum pH of 6.5. Both enzymes had an absolute requirement for Mg2+, required similar levels of ATP, and were not stimulated by added cyclic AMP or cyclic GMP. The pH 9.5 kinase was strongly inhibited by relatively low concentrations of GTP and CTP, but the pH 6.5 kinase was not affected. The pH 9.5 kinase phosphorylates the only two histidines (His-18 and His-75) in histone H4 to form 3-phosphohistidine. The pH 6.5 kinase phosphorylates the c-amino group of a lysine residue in histone I. Location of this lysine is not known. The phospho groups of both these derivatives are acid labile. 

Regulatory subunit of histone kinase 8-( Y-Carboxypropylthio)ade-nosine-3, S -cyclic phosphate Sepharose 4B with polylysine 171... 

Brizuela, L., G. Draetta D. Beach. 1989. Activation of human CDC2 protein as a histone HI kinase is associated with complex formation with the p62 subunit. Proc. Natl. Acad. Sci. USA 86 4362-6. 

Collas, P., T. Chang, C. Long J.M. Robl. 1995. Inactivation of histone HI kinase by Ca in rabbit oocytes. Mol. Reprod. Devel. 40 253-8. 

Sternberg, D.W., Scholz, G., Fukui, Y. Hanafusa, H. (1993). Activation of a histone Hi kinase by tyrosirre phosphorylation in v-src-transformed fibroblasts. EMBO ]., 12,323-30. Stevens, L (1986). Gene structure ar d organisation in the domestic fowl (Gallus domesticus). Worlds Poult. Sci.., 42, 232-42. 

---