Regulation of histone and beta A-globin gene expression during differentiation of chicken erythroid cells.

Affolter, Markus; Côté, J; Renaud, J; Ruiz-Carrillo, Adolfo

doi:10.1128/mcb.7.10.3663

Cited by 47 publications

(47 citation statements)

References 41 publications

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“…The most dramatic effect of a H1 histone variant, histone H5, has been observed in chicken erythrocytes, where it is progressively deposited onto the chromatin as the erythrocyte matures (22,23). This process is marked by the concomitant loss of H1 histones already bound to the chromatin, condensation of the chromatin, and an increase in nucleosome spacing.…”

Section: Overexpression Of H1mentioning

confidence: 99%

Effects of H1 Histone Variant Overexpression on Chromatin Structure

Gunjan¹,

Alexander²,

Sittman³

et al. 1999

Journal of Biological Chemistry

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The importance of histone H1 heterogeneity and total H1 stoichiometry in chromatin has been enigmatic. Here we report a detailed characterization of the chromatin structure of cells overexpressing either H1 0 or H1c. Nucleosome spacing was found to change during cell cycle progression, and overexpression of either variant in exponentially growing cells results in a 15-base pair increase in nucleosome repeat length. H1 histones can also assemble on chromatin and influence nucleosome spacing in the absence of DNA replication. Overexpression of H1 0 and, to a lesser extent, H1c results in a decreased rate of digestion of chromatin by micrococcal nuclease. Using green fluorescent protein-tagged H1 variants, we show that micrococcal nuclease-resistant chromatin is specifically enriched in the H1 0 variant. Overexpression of H10 results in the appearance of a unique mononucleosome species of higher mobility on nucleoprotein gels. Domain switch mutagenesis revealed that either the N-terminal tail or the central globular domain of the H1 0 protein could independently give rise to this unique mononucleosome species. These results in part explain the differential effects of H1 0 and H1c in regulating chromatin structure and function.

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Section: Overexpression Of H1mentioning

confidence: 99%

Effects of H1 Histone Variant Overexpression on Chromatin Structure

Gunjan¹,

Alexander²,

Sittman³

et al. 1999

Journal of Biological Chemistry

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“…Although the h5 gene is already set in an active chromatin conformation in early erythroid precursors (69), its transcription is not activated until the preerythroblast-to-erythroblast transition (2,72), coincident with the decline in the proliferation potential of the cells. The mechanisms that bring about transcriptional activation of the h5 gene are not fully elucidated but appear to reflect alterations in the balance between positive and negative effectors.…”

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confidence: 99%

Initiation Binding Receptor, a Factor That Binds to the Transcription Initiation Site of the Histone h5 Gene, Is a Glycosylated Member of a Family of Cell Growth Regulators

Gómez-Cuadrado

Martin

Noël

et al. 1995

Molecular and Cellular Biology

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Initiation binding receptor (IBR) is a chicken erythrocyte factor (apparent molecular mass, 70 to 73 kDa) that binds to the sequences spanning the transcription initiation site of the histone h5 gene, repressing its transcription. A variety of other cells, including transformed erythroid precursors, do not have IBR but a factor referred to as IBF (68 to 70 kDa) that recognizes the same IBR sites. We have cloned the IBR cDNA and studied the relationship of IBR and IBF. IBR is a 503-amino-acid-long acidic protein which is 99.0% identical to the recently reported human NRF-1/␣-Pal factor and highly related to the invertebrate transcription factors P3A2 and erected wing gene product (EWG). We present evidence that IBR and IBF are most likely identical proteins, differing in their degree of glycosylation. We have analyzed several molecular aspects of IBR/F and shown that the factor associates as stable homodimers and that the dimer is the relevant DNA-binding species. The evolutionarily conserved N-terminal half of IBR/F harbors the DNA-binding/dimerization domain (outer limits, 127 to 283), one or several casein kinase II sites (37 to 67), and a bipartite nuclear localization signal (89 to 106) which appears to be necessary for nuclear targeting. Binding site selection revealed that the alternating RCGCRYGCGY consensus constitutes high-affinity IBR/F binding sites and that the direct-repeat palindrome TGCGCATGCGCA is the optimal site. A survey of genes potentially regulated by this family of factors primarily revealed genes involved in growth-related metabolism.Histone H5 is a specific linker histone of the erythroid lineage which is expressed during the maturation of embryonic and adult avian erythrocytes (reference 2 and references therein). The chromatin levels of H5 increase progressively following activation of the h5 gene, so that at the end of the maturation process, the stoichiometry of linker histones (H5 plus H1) per core histone octamer is more than 1 (5). The effects of ectopic expression of H5 in nonerythroid cells, to levels comparable to those found in erythrocytes, argues for a direct role of H5 in the condensation and inactivity of the erythrocyte nucleus (81,82).Although the h5 gene is already set in an active chromatin conformation in early erythroid precursors (69), its transcription is not activated until the preerythroblast-to-erythroblast transition (2, 72), coincident with the decline in the proliferation potential of the cells. The mechanisms that bring about transcriptional activation of the h5 gene are not fully elucidated but appear to reflect alterations in the balance between positive and negative effectors. Transcription of the h5 gene is regulated by a complex assortment of ubiquitous and blood cell-specific factors acting at the promoter and three differentiation-specific enhancers located upstream and downstream of the gene (72,73). Although the majority of these factors contribute to transcriptional activity, one of them, IBR, was found to repress h5 transcription in vitro (25). IB...

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“…Blots of total RNA from the same number of cells were hybridized with cDNA probes for H5, GATA-1, GATA-2, and GATA-3, labeled at comparable specific radioactivities. Figure 1OA (lane 1) shows that GATA-1 mRNA was, by and large, the most abundant mRNA in ND-HD3, followed by those of GATA-2 and GATA-3, the latter representing a relatively minor species. H5 mRNA, barely detectable in the autoradiography (lane 1), could be better seen when the blot was hybridized with the H5 probe alone.…”

Section: Resultsmentioning

confidence: 99%

“…Contrary to late erythroid markers, including the adult globin chains and cell surface proteins (2), H5 is already present in the early precursor CFU(E) (3,45), and its expression increases further with the onset of the expression of these late genes (1). Transcription run-on analysis of erythroid cells at different stages of maturation have also indicated that the activity of the H5 gene is lower in proliferating erythroid precursors than in more mature cells (1). Thus, H5 expression during maturation is predominantly regulated at the transcription level.…”

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confidence: 99%

Transcription of the histone H5 gene is regulated by three differentiation-specific enhancers.

et al. 1993

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Histone H5, an early marker of the avian erythroid lineage, is expressed at low levels in early erythroid precursors and at higher levels in more mature cells. We show that the increase in H5 expression is due to transcriptional activation of the H5 gene following differentiation of precursor CFU(E). We have found and characterized two upstream enhancers, El (between -2233 and -1878 from the site of transcription initiation, +1) and E3 (between -1321 and -1163), and confirmed the presence of a downstream enhancer (C. D.Trainor, S. J. Stamler, and J. D. Engel, Nature [London] 328:827-830, 1987) E7 (between +846 and + 1181) which are responsible for the increase in H5 gene transcription. The enhancers had a weak effect in nondifferentiated CFU(E) but a strong effect when the cells were induced to differentiate. Cooperation among the three enhancers, however, was not required for HS gene activity in the differentiated cells. The enhancers contain binding sites for several ubiquitous and erythroid cell-specific nuclear proteins, including GATA-1, as demonstrated with GATA-1-specific antibodies. Although the GATA sites were required for enhancer function, the concentration of GATA-1, GATA-2, and GATA-3 decreased during cell differentiation, and overexpression of these factors had little effect on H5 transcription. Hence, the differentiation-specific effect of the enhancers is not mediated by changes in relative levels of the GATA factors. Functional analysis of the H5 promoter indicated that the requirement of several elements, including a GC box necessary for transcription enhancement, did not change during the early stages of CFU(E) differentiation. However, the UPE, a positive element in proliferating CFU(E) recognized by the transcription factor H4TF2, was dispensable in the differentiated cells. These results suggest that as the cells enter the final stages of differentiation, there is a reprogramming of the regulatory factors that control H5 transcription and that the enhancers rescue and increase the activity of the promoter.Vertebrate erythropoiesis is characterized by the expression of sets of tissue-specific genes which are temporally regulated during maturation of the committed precursors. The chicken histone H5 gene is an interesting marker by which to study how these processes are regulated, because it responds both to early and late differentiation cues during erythropoiesis. Contrary to late erythroid markers, including the adult globin chains and cell surface proteins (2), H5 is already present in the early precursor CFU(E) (3, 45), and its expression increases further with the onset of the expression of these late genes (1). Transcription run-on analysis of erythroid cells at different stages of maturation have also indicated that the activity of the H5 gene is lower in proliferating erythroid precursors than in more mature cells (1). Thus, H5 expression during maturation is predominantly regulated at the transcription level.In an attempt to understand the molecular mechanisms accounting for the t...

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Regulation of histone and beta A-globin gene expression during differentiation of chicken erythroid cells.

Cited by 47 publications

References 41 publications

Effects of H1 Histone Variant Overexpression on Chromatin Structure

Effects of H1 Histone Variant Overexpression on Chromatin Structure

Initiation Binding Receptor, a Factor That Binds to the Transcription Initiation Site of the Histone h5 Gene, Is a Glycosylated Member of a Family of Cell Growth Regulators

Transcription of the histone H5 gene is regulated by three differentiation-specific enhancers.

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