Phosphorylation of non-histone proteins in the regulation of chromosome structure and function

Kleinsmith, Lewis J.

doi:10.1002/jcp.1040850412

Cited by 144 publications

(37 citation statements)

References 46 publications

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Section: Introductionmentioning

confidence: 99%

“…In view of their general lack of species and tissue specificity, histones are now thought to play primarily structural roles (21), thereby resulting in general template restriction. In contrast, nonhistone proteins by virtue of their heterogeneity and tissue and species specificity may participate more specifically in gene regulation (14,21 (27).Application of the synthetic auxin, 2,4-D, to etiolated soybean seedlings causes very large increases in RNA synthesis in the mature region of the hypocotyl (13). Ribosomal RNA is preferentially synthesized in response to 2,4-D treatment (10, 13), and this increase is associated with a 5-to 8-fold increase in RNA polymerase I activity (8).…”

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confidence: 99%

“…Since the initial observation that proteins isolated from lymphocyte nuclei were rich in phosphoserine (16), numerous correlations between increased chromosomal protein phosphorylation and gene activity have been observed (14). Transcription of rat liver chromatin by homologous RNA polymerase is stimulated by the addition of nonhistone phosphoprotein but not affected by dephosphorylated nonhistone protein (33).…”

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confidence: 99%

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2,4-Dichlorophenoxyacetic Acid-enhanced Phosphorylation of Soybean Nuclear Proteins

Murray

Key²

1978

Plant Physiol.

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In vitro nuclear protein phosphorylation is enhanced i nuclei isolated from 2,4-dkcorophenoxyacetic acid (2,4-D)-treated mature soybean (Glycine mar) hypocotyl reltive to nuclei from untreated tise. Evidence derived in numerous systems is compatible with the hypothesis that at least some chromosomal proteins participate in transcriptional regulation. Changes in the types and quantities and various modifications of these proteins (e.g. methylation, acetylation, phosphorylation, and thiolation) occur during passage through the cell cycle and during periods of increased template transcription (for reviews, see refs. 14 and 21). Histones were first shown to restrict template activity in 1962 (9). In view of their general lack of species and tissue specificity, histones are now thought to play primarily structural roles (21), thereby resulting in general template restriction. In contrast, nonhistone proteins by virtue of their heterogeneity and tissue and species specificity may participate more specifically in gene regulation (14,21 (27).Application of the synthetic auxin, 2,4-D, to etiolated soybean seedlings causes very large increases in RNA synthesis in the mature region of the hypocotyl (13). Ribosomal RNA is preferentially synthesized in response to 2,4-D treatment (10, 13), and this increase is associated with a 5-to 8-fold increase in RNA polymerase I activity (8). While auxin does increase the synthesis of all species of RNA including short lived mRNA and heterodisperse nuclear RNA (13), RNA polymerase II activity is enhanced less than 30% if at all (8). While increased RNA polymerase I activity may account for the increase in rRNA synthesis, changes in the level of RNA polymerase II alone do not seem sufficient to explain the increased synthesis of heterodisperse nuclear RNA and mRNA. Alteration of chromatin template availability is one mechanism by which 2,4-D could affect the synthesis of informational RNA without requiring increased RNA polymerase II activity. Such a model would be consistent with results indicating that chromatin isolated from IAA-treated lentil roots is more available for in vitro transcription by RNA

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Section: Introductionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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2,4-Dichlorophenoxyacetic Acid-enhanced Phosphorylation of Soybean Nuclear Proteins

Murray

Key²

1978

Plant Physiol.

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“…Sci. USA 75 (1978) sociated with chromatin appears to be important in regulating gene expression (34,35). cAMP and cGMP have been observed to modify the phosphorylated state of various fractions of chromosomal proteins (36)(37)(38), including RNA polymerase I from lymphocyte nuclei (39) and RNA polymerase II in nuclear extracts from mammary gland (40).…”

Section: Discussionmentioning

confidence: 99%

Association of cyclic GMP with gene expression of polytene chromosomes of Drosophila melanogaster.

Spruill¹,

Hurwitz²,

Lucchesi³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

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The distribution of cyclic nucleotides on polytene chromosomes isolated from Drosophila melanogaster salivary glands was examined by using an indirect immunofluorescent technique. With a fixative that minimized the loss of chromosomal proteins, cyclic GMP, but not cyclic AMP, was observed distributed along the chromosomes. The subchromosomal distribution of cyclic GMP correlated with genetically active sites on the chromosomes. After heat-shock treatments, the intensity of cyclic GMP fluorescence was markedly enhanced at specific loci on the chromosomes, with locus 93D as the most intensely fluorescent. Autoradiographic analysis with [3Hjuridine revealed that 93D was the most transcriptionally active locus within a particular nucleus. These observations suggest that cyclic GMP may participate in processes associated with transcription on polytene chromosomes. The involvement of cyclic GMP in nuclear events associated with gene expression is discussed.Cyclic nucleotides have been implicated as intracellular mediators during processes associated with growth in mammalian tissues and animal cells in culture (1, 2). Utilizing an immunocytochemical approach (3, 4), we have examined the distribution of adenosine 3':5'-cyclic monophosphate (cAMP) and guanosine 3':5'-cyclic monophosphate'(cGMP) during growth and/or differentiation in several biological systems (5-7). The consistent localization of cGMP fluorescence in association with nuclear elements in several tissues (5-9) suggested that cGMP was involved in nuclear events in these cells. Of particular interest was the observation of cGMP along the autosomal bivalents of pachytene spermatocytes during the meiotic prophase in rat testis (6,8). Autoradiographic studies in mouse testis (10) have demonstrated a peak of RNA synthesis during the middle pachytene stage. These observations suggested that cGMP might be involved in processes associated with RNA synthesis in these cells.In order to assess further the possible involvement of cyclic nucleotides with transcriptive activities, we have utilized polytene chromosomes from Drosophila salivary glands, a valuable system for studying transcription. The distribution of cyclic nucleotides on polytene chromosomes was examined immunocytochemically to determine if changes in the distribution occurred concurrently with changes in genetic activities at specific loci. Because chromosomal puffing at specific loci is observed during normal development (11) and can be induced by hormone (12) or environmental stimuli (13,14), this system offers the advantage of being able to visualize changes in gene activity (i.e., puffing) under various conditions.In several recent reports, immunocytochemical methods were presented for determining the distribution of chromosomal proteins (15-17), including RNA polymerase 11 (17), on Drosophila polytene chromosomes. We adapted these methods to the localization of cyclic nucleotides on polytene chromosomes. cGMP fluorescence was observed to be distributed along the chromosome arms whereas cAMP...

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“…Only ATP organisms (14, 22). Evidence that chromosomal protein phosphorylation may be involved in the regulation of eukaryotic gene transcription has stimulated interest in nuclear protein kinases (13). Correlations exist between protein kinase activity and the activation of RNA synthesis, and high levels of protein kinase activity can be isolated with transcriptionally active chromatin (10, 20; refs.…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of a Chromatin-associated Protein Kinase from Soybean

Murray¹,

Guilfoyle²,

Key³

1978

Plant Physiol.

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A chromatin-associated casein-type protein kinase has been purified 500-fold from soybean ( Glycine max, var. Wayne) tissue. The enzyme can be completely dissociated from isolated chromatin in 250 millimolar (NH4)2SO4. After purification, the kinase preparation is stable for at least 6 months at 0 C. The enzyme will phosphorylate casein, phosvitin, and denatured chromatin proteins, but not histones. Only ATP organisms (14, 22). Evidence that chromosomal protein phosphorylation may be involved in the regulation of eukaryotic gene transcription has stimulated interest in nuclear protein kinases (13). Correlations exist between protein kinase activity and the activation of RNA synthesis, and high levels of protein kinase activity can be isolated with transcriptionally active chromatin (10, 20; refs. in 26). Modifications of RNA polymerase activity by protein kinases have been reported in several systems including Ascites tumors (5) and calf thymus (9).Protein kinase activities described in animal systems may be divided into two classes according to substrate specificity and the requirement for cAMP or cGMP for expression of maximal activity. Cyclic nucleotide-dependent protein kinases are especially active on histones but generally will not phosphorylate acidic proteins. Because the majority of the cyclic nucleotidedependent protein kinase activity is found in the cytosol and/or membrane fractions, they appear to be primarily extranuclear (10,14,22 (refs. in 26). In addition, protein kinase activities have been detected in nuclei, ribosomes, and chloroplasts from a number ofhigher plants (refs. in 26). However, no casein kinase has been extensively purified or characterized from nuclei or chromatin of higher plants.Concomitant with auxin-enhanced RNA synthesis in soybean hypocotyls (11) there is an increase in nuclear protein phosphorylation and in nuclear casein kinase activity (21). Moreover, RNA polymerase preparations from soybean were found to copurify with a protein kinase activity during the early stages of purification (unpublished). Purification of this enzyme was undertaken in order to compare its activity to that of the casein kinases described in animal systems and to test for a possible role of protein phosphorylation in the regulation of RNA synthesis in soybean hypocotyls. Soybean hypocotyl tissue contains a histone kinase (16) in addition to the chromatin-associated casein-type kinase which will be described here. This study shows that the properties of soybean casein kinase are similar to casein-type kinases found in animal systems. METHODSProtein Kinase Assays. Carrier-free according to Schendel and Wells (23). Standard protein kinase assays contained, in a final volume of 0.2 ml, 100 mm Tris-HCl (pH 7.5), 10 mm MgCl2, 10 mM DTT, 25 uM ATP cpm/pmol), and 500 ,ug/ml of a-casein (Sigma). Assays were initiated with 5 ul of protein kinase preparation, incubated for 30 min at 28 C, and terminated with 3 ml of cold 10%o (w/v) trichloroacetic acid containing 10 mm sodium pyrophosphate....

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Phosphorylation of non-histone proteins in the regulation of chromosome structure and function

Cited by 144 publications

References 46 publications

2,4-Dichlorophenoxyacetic Acid-enhanced Phosphorylation of Soybean Nuclear Proteins

2,4-Dichlorophenoxyacetic Acid-enhanced Phosphorylation of Soybean Nuclear Proteins

Association of cyclic GMP with gene expression of polytene chromosomes of Drosophila melanogaster.

Isolation and Characterization of a Chromatin-associated Protein Kinase from Soybean

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