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D Doenecke

Publications and source records attributed to D Doenecke.

At least 73 records · Page 4Linked to original sources
PubMed1992

Differential expression of the histone H1 zero gene in U937 and HL-60 leukemia cell lines.

The expression of the human H1 zero histone gene and of a main type H1 gene was analyzed in two human leukemia cell lines. The main type, replication dependent H1 gene expression reflected the state of proliferation of both cell lines. No H1 zero mRNA was detected in the promyelocytic HL-60 line, whereas the monocytic U937 cells showed low steady-state levels of 1H zero mRNA. Stimulation of HL-60 with several known inducers of differentiation failed to induce any accumulation of H1 zero mRNA. Treatment of U937 with phorbol ester or butyrate, on the other hand, led to an increase of the H1 zero mRNA concentration.

Butyrates↗
PubMed1992

Expression of a histone H1 gene (H1.1) in human testis and Hassall's corpuscles of the thymus. Expression of a histone H1 gene (H1.1).

The expression of a H1 gene (H1.1) was studied in several human tissues. Northern blot analysis revealed that this gene is expressed in testis and thymus, but not in other human tissues like liver, spleen, lung, brain, thyroid gland and skin fibroblasts. Furthermore in situ hybridization on tissue sections revealed a cell type specific expression of histone H1.1 gene in the Hassall's corpuscles of the thymus.

Gene Expression↗
PubMed1991

Structure and expression of the human gene encoding testicular H1 histone (H1t).

The gene coding for the human H1t histone, a testis-specific H1 subtype, was isolated from a genomic library using a human somatic H1 gene as a hybridization probe. The corresponding mRNA is not polyadenylated and encodes a 206-amino-acid protein. Sequence analysis and S1 nuclease mapping of the human H1t gene reveals that the 5' flanking region contains several consensus promoter elements, as described for somatic, i.e., S-phase-dependent H1 subtype genes. The 3' region includes the stem-and-loop structure necessary for mRNA processing of most histone mRNAs. Northern blot analysis with RNAs from different human tissues and cell lines revealed that only testicular RNA hybridized with this gene probe.

Amino Acid Sequence↗
PubMed1991

Regulation of histone H5 and H1 zero gene expression under the control of vaccinia virus-specific sequences in interferon-treated chick embryo fibroblasts.

The duck histone H5 and human H1 zero were inserted into the thymidine kinase (TK) gene of vaccinia virus and the interferon sensitivity of their expression under the control of the viral TK and P7.5 promoters in chick embryo fibroblasts (CEF) was compared to the interferon sensitivity of vaccinia virus WR specific TK induction. Expression and transport of these histones to the nucleus in CEF infected with the appropriate vaccinia virus recombinants could be detected with antisera raised against chick histone H5. In CEF cultivated for 3 days, interferon treatment that completely inhibited TK synthesis had no or only a marginal inhibitory effect on the expression of the histone genes. Inhibition of the expression of the histones could be detected under conditions of increased interferon sensitivity in aged CEF. The magnitude of inhibition was, however, less pronounced than the inhibition of viral TK synthesis. These data indicate that flanking vaccinia virus DNA regions confer interferon sensitivity to the expression of these histone genes, but that they contain structural information that partially exempts their expression from the inhibitory activity of the interferon-induced regulatory system.

Animals↗
PubMed1991

Isolation and characterization of two human H1 histone genes within clusters of core histone genes.

Two human H1 histone genes, termed H1.3 and H1.4, were isolated from two cosmid clones. The H1.4 gene is associated with an H2B gene, whereas genes coding for all four core histones are located in the vicinity of the H1.3 gene. This cluster arrangement was found both in the two cosmid clones and on overlapping bacteriophage clones isolated from an EMBL3 library. In continuation of our previous analysis of two human H1 genes, this analysis raises the number of completely sequenced H1 histone genes within clusters of core histone genes to four.

Amino Acid Sequence↗
PubMed1990

Effects of antineoplastic phospholipids on parameters of cell differentiation in U937 cells.

The proliferation of the human promonocytic leukemia cell line U937 is inhibited by several ether lipids, ether lipid analogues and by phorbol esters. An early effect of this retardation of cell growth is the induction of a basic chromosomal protein, histone H1(0). Northern blot analysis of H1(0) mRNA levels reveals an increase of the mRNA concentration within a few hours after addition of hexadecylphosphocholine and 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine. This early effect on the synthesis of a subtype of H1 proteins precedes the expression of several parameters of the monocytic differentiation of U937 cells.

Antigens, Surface↗
PubMed1990

Increased level of histone H1(0) messenger RNA in hypoxic Ehrlich ascites tumor cells.

We have investigated the expression of the H1 histone subtype H1(0) gene in Ehrlich ascites tumor cells (EAT) under varied conditions of oxygen supply. Our results show that proliferating EAT cells express H1(0) mRNA at a basal level under normoxic conditions. Severe hypoxia leads to a cessation of cell growth and causes an accumulation of cells in G1. Here, we show that the level of H1(0) histone mRNA increases within a few hours after the onset of hypoxia.

Animals↗
PubMed1990

The expression of the histone H1 (0) gene in the human hepatoma cell line HepG2 is independent of the state of cell proliferation.

The H1 histone subtype H1 (0) is a characteristic component of the chromatin of several mammalian tissues. Since H1 (0) is synthesized in nondividing cells upon terminal differentiation, it has been mostly considered either as a prerequisite for or as a consequence of an arrest of DNA replication during the process of differentiation. In several H1 (0)-expressing systems studied until now, inducers of differentiation or inhibitors of DNA synthesis cause an increase of the ratio between H1 (0) and the other H1 proteins. We have studied the steady-state levels of histone H1 (0) mRNA under varied growth conditions in the human hepatoma cell lines HepG2 and Hep3B, and we show in the HepG2 system that H1 (0) is not confined to resting cells, that the H1 (0) gene appears to be expressed throughout the cell cycle and that established inducers of de novo H1 (0) synthesis fail to cause a further increase of the high H1 (0) level. This constitutive expression of H1 (0) appears to reflect the chromatin structure of the liver cells, from which the HepG2 hepatoblastoma cells initially may have evolved. In contrast to the situation in nondividing adult liver cells, the H1 (0) gene is transcribed in HepG2 at a high level, and this expression is compatible with DNA replication.

Butyrates↗
PubMed1989

Conserved organization of an avian histone gene cluster with inverted duplications of H3 and H4 genes.

The organization of histone gene clusters of the duck Cairina moschata was studied in the DNA inserts of two recombinant phage that overlap and feature identical histone gene arrangements but differ in sequence details and in the extent of repetition of an AT-rich motif in one of the nontranscribed spacer regions. These few but substantial differences between otherwise nearly identical histone gene groups suggest that we have independently isolated alleles of the same site of the duck genome or that this gene arrangement occurs (with slight variations) more than once per haploid genome. Within the histone gene cluster described, H3 and H4 genes are duplicated (with inverted orientation), whereas one H1 gene is flanked by single H2A and H2B genes. The arrangement of duck histone genes described here is identical to a subsection of the chicken genome but differs from any other published histone gene cluster.

Amino Acid Sequence↗
PubMed1989

Human H1 histones: conserved and varied sequence elements in two H1 subtype genes.

The genes coding for two different human H1 histones were isolated, and the primary structures were deduced from the nucleotide sequences. The genes differ from each other and from any other vertebrate H1 structure described until now. The differences occur mainly within the N- and C-terminal H1 domains, whereas the central part of the protein is highly conserved. Within the flanking domains, however, some sequence elements are shared by different H1 subtype genes. An octapeptide, which has been described in C-terminal domains of most H1 histones, is found in both H1 subtypes. The nucleotide sequences of the flanking portions of both H1 genes show conserved motifs at established regulatory sites, but otherwise these 3' and 5' noncoding sequences of both genes differ substantially.

Amino Acid Sequence↗
PubMed1988

Early increase in histone H1(0) mRNA during differentiation of F9 cells to parietal endoderm.

We have isolated and characterized cDNA clones coding for the H1 histone subtype H1(0) in mouse teratocarcinoma cells. The mRNA is 2100 nt long and contains a coding sequence which is highly related to that of the human H1(0) gene. Using this cDNA as a probe, we have shown that, in comparison to undifferentiated F9 cells, differentiated F9 teratocarcinoma cells contain large amounts of H1(0) mRNA. This increase takes place very early during differentiation and does not correlate with changes in the rate of cell division. This indicates that the accumulation of H1(0) mRNA is not the result of reduced proliferation. Most likely on the contrary, the increase in the amount of H1(0) and the resulting effects on the formation of high order chromatin structures are parts of the differentiation program induced in F9 cells.

Amino Acid Sequence↗
PubMed1988

The H1 and core histone subtypes: differential gene expression and varied primary structures.

The patterns of chromosomal proteins reflect in many cases the functional state of the respective cell type. The H1 histone group is particularly important in this respect, since these histones are involved in the higher order chromatin organization above the level of chains of nucleosomes. In mammals, the H1 histone family comprises at least five main subtypes (H1a-H1e), a testicular variant (H1t) and, thirdly, a subtype H1(0), which is found only in terminally differentiated cells. The H1(0) variant is structurally related to the avian red blood cell specific histone H5, which was the basis for our recent isolation of the human H1(0) gene. Changes of H1 histone patterns may be crucial events in modulating local chromatin arrangements, since the formation of higher order chromatin structures depends on a cooperative interaction of the H1 histones. Variations in their patterns can be studied in vivo during several developmental processes (such as spermatogenesis, erythropoiesis, maturation of several cell types) or in vitro in several tumor cell lines upon treatment with several inducers or upon inhibition of cell division. The differential regulation of the individual H1 subtypes is reflected in the gene and mRNA structures coding for the respective proteins. The cell cycle regulated histones are mostly encoded by non-polyadenylated mRNAs, whereas H5 as well as H1(0) mRNA shows a poly(A) tail at its 3' end. In conclusion, gene activity may not only be controlled at the level of RNA polymerases and their regulatory transcription factors. The varied patterns of chromosomal proteins at different stages during development and differentiation suggest that the local or overall organization of chromatin plays an additional role in these regulatory programs. Hence, the analysis of variations in patterns of chromosomal proteins is an integral part of the investigation of gene regulation mechanisms.

Amino Acid Sequence↗
PubMed1987

A highly conserved sequence in H1 histone genes as an oligonucleotide hybridization probe: isolation and sequence of a duck H1 gene.

A 3.5-kb HindIII fragment of a histone gene cluster was isolated from a recombinant phage out of a duck genomic library. This DNA contains a duck H1 gene and its flanking sequences. The hybridization probe, which was used to screen for the H1 gene, had been designed on the basis of a comparative analysis of available H1 gene and protein data. Most H1 histones contain repeated motifs in their C-terminal domain, and these form part of an octapeptide (ser pro lys lys ala lys lys pro) that is highly conserved in many H1 histone proteins. A comparison of the duck H1 described here with two different published chicken H1 histone sequences reveals conservative amino acid exchanges at 22 (of 217 and 218, respectively) positions. The homology is maintained at the flanking sequences, and includes the putative H1 histone gene-specific signal structures and the established 3' stem and loop structures and the CAAGA box. The duck H1 gene and its flanking sequence have been found in identical arrangements in two recombinant bacteriophages, but minor sequence variations and genomic Southern blotting after HindIII digestion suggest that we have either isolated alleles of this genome segment or that the gene described may occur twice per haploid duck genome.

Amino Acid Sequence↗
PubMed1986

Butyrate induced accumulation of a 2.3 kb polyadenylated H1(0) histone mRNA in HeLa cells.

Sodium butyrate was used to induce the accumulation of human H1(0) mRNA in HeLa cells. The length of this mRNA (2,300 nucleotides) was determined by Northern blot hybridization and S1 nuclease analysis using a human H1(0) gene probe. The mRNA shows long 5' and 3' non coding segments and it is polyadenylated. The signal for this step of mRNA maturation (cleavage and polyadenylation) appears to be the hexanucleotide AAUAAA in analogy to most (other than histone) mRNA species. Thus, the mode of maturation of H1(0) mRNA differs, on one hand, from that of the cell cycle dependent mRNA species, where it is based on a specific stem-and-loop structure. On the other hand, the 3' end of H1(0) mRNA varies from H5 mRNA, which is characterized by two unique dyad symmetry structures at its 3' end.

Base Sequence↗
PubMed1986

Differential distribution of lysine and arginine residues in the closely related histones H1 and H5. Analysis of a human H1 gene.

A human H1 histone gene and its flanking sequences were isolated from a human gene library using a fragment of the duck H5 histone gene as a hybridization probe. The primary structure of this human H1 histone (as deduced from the nucleotide sequence of the gene) reveals a close homology of H1 and H5 histones and fits the three-domain organization of all members of the H1 histone family. Within this protein organization, the C-terminal domain of H1 differs from the arginine-rich H5 in its distribution of the basic amino acids: the C-terminal domain of the human H1 shows only one arginine and most of the H5 specific arginine positions show lysine instead.

Amino Acid Sequence↗