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Histone kinase

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. [Pg.43]

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 ... [Pg.137]

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... [Pg.332]

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]. [Pg.216]

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]. [Pg.218]

HISTIDINOL-PHOSPHATE PHOSPHATASE HISTIDYL-tRNA SYNTHETASE HISTONE KINASE Hofmann rule,... [Pg.748]

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. [Pg.153]

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. [Pg.121]

Regulatory subunit of histone kinase 8-( Y-Carboxypropylthio)ade-nosine-3, S -cyclic phosphate Sepharose 4B with polylysine 171... [Pg.350]

VRKl, a member of the casein kinase I (Minshull et al. 1989) family is a serine/ threonine kinase related to vaccinia virus BIR seiine/threonine kinase (Klerkx et al. 2009), has been identified as an early response gene required for cyclin D1 expression. VRKl controls cell survival by phosphorylation of p53, chromatin condensation by phosphorylation of histone, and nuclear envelope assembly by phosphorylation of BANFl (Valbuena et al. 2011). It is also involved in fragmentation of Golgi apparatus in the G2 phase-cell cyde. In Drosophila oocytes, nucleosomal histone kinase-1 (Drosophila homolog of VRKl) regulates... [Pg.468]

Table 1). Two third of this eIF-2 kinase (PK-i) is in the cell sap and one third in ribosomal extracts, the latter containing most of protein 67 and 35 substrates (4) PK-i is not retained on DEAE-cellulose, elutes from phosphocellulose (pH6.7) at 330mMKCl, and from hydroxylapatite at 200mM phosphate overall purification was about 500- old. The endogenous protein 67 phosphorylation activity was still present in the purified PK-i (Figure 2) as well as a dsMA-dependent histone kinase selective for the arginine-rich... [Pg.240]


See other pages where Histone kinase is mentioned: [Pg.1]    [Pg.320]    [Pg.321]    [Pg.329]    [Pg.333]    [Pg.401]    [Pg.401]    [Pg.342]    [Pg.725]    [Pg.221]    [Pg.120]    [Pg.296]    [Pg.266]    [Pg.588]   
See also in sourсe #XX -- [ Pg.322 , Pg.323 , Pg.403 ]

See also in sourсe #XX -- [ Pg.119 ]




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