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PubMed2001

Signals from the ventral midline and isthmus regulate the development of Brn3.0-expressing neurons in the midbrain.

The vertebrate midbrain consists of dorsal and ventral domains, the tectum and tegmentum, which execute remarkably different developmental programs. Tectal development is characterized by radial migration of differentiating neurons to form a laminar structure, while the tegmentum generates functionally diverse nuclei at characteristic positions along the neural axis. Here we show that neurons appearing early in the development of the tectum are characterized either by the expression of the POU-domain transcription factor Brn3.0, or by members of the Pax and LIM families. Early neurons of the rostral tegmentum co-express Brn3.0 and Lim1/2, and caudal tegmental neurons express Islet1/2. Notochord tissue or Shh-transfected epithelial cells, transplanted to the developing tectum, suppress the development of tectal neurons, and induce the differentiation of multiple tegmental cell types. The distance from the midbrain-hindbrain boundary (MHB) determines the specific markers expressed by the tegmental neurons induced in the tectum, and the transplantation of MHB tissue adjacent to the rostral tegmentum also induces caudal markers, demonstrating the role of MHB signals in determining the phenotype of these early midbrain neurons. Co-culture of isolated midbrain neuroepithelium with Shh-expressing cells demonstrates that Shh is sufficient to convert tectal neurons to a tegmental fate. In mice lacking Shh, Brn3.0- and Pax7-expressing neurons typical of the tectum develop throughout the ventral midbrain, and gene expression patterns characteristic of early tegmental development do not appear.

Animals↗
PubMed1998

Progenitor cells in the adult zebrafish nervous system express a Brn-1-related POU gene, tai-ji.

The adult fish brain undergoes continuous neurogenesis and retains the capacity to regenerate. However, the cellular and molecular basis of this process is not well understood. We report on the cloning and characterization of a Brain-1-related, class III POU domain gene, tai-ji, in the developing and adult zebrafish, as well as in a human cell line, hNT2. During development, as differentiation occurs, the expression of tai-ji is downregulated in the notochord, muscle, nervous system and dorsal fin. Similarly, tai-ji is expressed in the human neuronal precursor cell, hNT2, but is downregulated upon differentiation with retinoic acid. In the adult zebrafish nervous system, tai-ji persists in germinal zones, including cells in the germinal zone of the retina, the basal cells of the olfactory epithelium and cells of the subependymal zones in the optic tectum and telencephalon. Subsets of the tai-ji-expressing cells in these regions incorporate BrdU. Most of the tai-ji-expressing cells within these regions of the zebrafish brain are not differentiated and do not express a marker for post-mitotic neurons, acetylated tubulin nor do they express a marker of glial cells, glial acidic fibrillary protein (GFAP). We propose that the majority of the tai-ji-expressing cells are neural stem or progenitor cell populations that may represent the cellular basis for continuous growth in the adult nervous system.

Animals↗
PubMed1999

The POU domain gene, XlPOU 2 is an essential downstream determinant of neural induction.

The POU domain gene, XlPOU 2, acts as a transcriptional activator during mid-gastrulation in Xenopus. Overexpression or misexpression of VP16-POU-GR, a fusion protein consisting of the strong activator domain of VP16 and the POU domain of XlPOU 2, results in ectopic expression of the neural-specific genes, nrp-1, en-2, and beta-tubulin. In contrast, overexpressing a dominant-inhibitory form of XlPOU 2 inhibits the chordin-induced neuralization of uncommitted ectoderm, and results in a loss of nrp-1 and en-2 expression in embryos. Furthermore, in uncommitted ectoderm, XlPOU 2 regulates the developmental neural program that includes a number of pre-pattern genes and at least one proneural gene, X-ngnr-1, thus playing a key role during neural determination.

Animals↗
PubMed2002

Diverse adaptations of an ancestral gill: a common evolutionary origin for wings, breathing organs, and spinnerets.

Changing conditions of life impose new requirements on the morphology and physiology of an organism. One of these changes is the evolutionary transition from aquatic to terrestrial life, leading to adaptations in locomotion, breathing, reproduction, and mechanisms for food capture. We have shown previously that insects' wings most likely originated from one of the gills of ancestral aquatic arthropods during their transition to life on land. Here we investigate the fate of these ancestral gills during the evolution of another major arthropod group, the chelicerates. We examine the expression of two developmental genes, pdm/nubbin and apterous, that participate in the specification of insects' wings and are expressed in particular crustacean epipods/gills. In the horseshoe crab, a primitively aquatic chelicerate, pdm/nubbin is specifically expressed in opisthosomal appendages that give rise to respiratory organs called book gills. In spiders (terrestrial chelicerates), pdm/nubbin and apterous are expressed in successive segmental primordia that give rise to book lungs, lateral tubular tracheae, and spinnerets, novel structures that are used by spiders to breathe on land and to spin their webs. Combined with morphological and palaeontological evidence, these observations suggest that fundamentally different new organs (wings, air-breathing organs, and spinnerets) evolved from the same ancestral structure (gills) in parallel instances of terrestrialization.

Adaptation, Physiological↗
PubMed2003

The herpes simplex virus VP16-induced complex: the makings of a regulatory switch.

When herpes simplex virus (HSV) infects human cells, it is able to enter two modes of infection: lytic and latent. A key activator of lytic infection is a virion protein called VP16, which, upon infection of a permissive cell, forms a transcriptional regulatory complex with two cellular proteins - the POU-domain transcription factor Oct-1 and the cell-proliferation factor HCF-1 - to activate transcription of the first set of expressed viral genes. This regulatory complex, called the VP16-induced complex, reveals mechanisms of combinatorial control of transcription. The activities of Oct-1 and HCF-1 - two important regulators of cellular gene expression and proliferation - illuminate strategies by which HSV might coexist with its host.

Animals↗
PubMedDate not supplied

Similarities and differences among inner retinal neurons revealed by the expression of reporter transgenes controlled by Brn-3a, Brn-3b, and Brn-3c promotor sequences.

Brn-3a, Brn-3b, and Brn-3c are highly homologous POU-domain transcription factors that are expressed in subsets of retinal ganglion cells. From each of the mouse Brn-3 genes, a DNA segment ranging in size from 4.6 to 13.4 kb and located immediately upstream of the start site of translation was joined to a human placental alkaline phosphatase (AP) reporter cDNA. Following the introduction of each construct into the mouse germline, a total of 19 transgenic lines were obtained, of which 16 expressed the AP reporter in the retina. Unexpectedly, at least 14 of the 16 expressing lines showed AP activity in subsets of amacrine cells, and these subsets typically differed among mouse lines injected with the same construct. Transgene expression was also found in ganglion cells in four lines and bipolar cells in seven lines. In all cases AP activity was confined to cells in the inner nuclear layer and the ganglion cell layer. The expression of Brn-3 transgenes in multiple cell types in the inner retina is reminiscent of earlier experiments in which visual pigment transgenes were found to be expressed in multiple cell types in the outer retina. Taken together, these observations suggest that anatomically and/or functionally related retinal neurons contain partially overlapping transcriptional regulatory specificities.

Alkaline Phosphatase↗
PubMed1993

Pit-1/GHF-1 binds to TRH-sensitive regions of the rat thyrotropin beta gene.

Three regions within the 5'-flanking region of the TSH beta gene have A-T-rich sequences which have sequence similarity to binding sites for the pituitary-specific POU domain transcription factor Pit-1/GHF-1. These three regions have been termed TSH A (-274 to -258 bp), TSH B (-336 to -326 bp), and TSH C (-402 to -384 bp). TSH A and TSH C are able to confer 2-6-fold TRH stimulation to the heterologous viral thymidine kinase (tk) promoter in transient expression assays in GH3 pituitary cells; TSH C can confer a 3-10-fold increase in basal enhancer activity as well. TSH A, B, and C DNAs all bound Pit-1 from GH3 cell nuclear extracts, based on gel mobility shift analysis in which antibody against Pit-1 prevented the formation of specific DNA-GH3 nuclear protein complexes. TSH A and TSH C also each formed several additional DNA-nuclear protein complexes which were not observed with TSH B. Some of these complexes may contain Pit-1 as their formation was inhibited by the addition of Pit-1 antibody; other complexes, however, were not altered by antibody treatment. All three A-T-rich elements bound in vitro translated Pit-1, with calculated affinities of 360 (A), 125 (B), and 38 (C) nM, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1990

Dwarf locus mutants lacking three pituitary cell types result from mutations in the POU-domain gene pit-1.

Mutations at the mouse dwarf locus (dw) interrupt the normal development of the anterior pituitary gland, resulting in the loss of expression of growth hormone, prolactin and thyroid-stimulating hormone, and hypoplasia of their respective cell types. Disruptions in the gene encoding the POU-domain transcription factor, Pit-1, occur in both characterized alleles of the dwarf locus. The data indicate that Pit-1 is necessary for the specification of the phenotype of three cell types in the anterior pituitary, and directly link a transcription factor to commitment and progression events in mammalian organogenesis.

Amino Acid Sequence↗
PubMed1991

I-POU: a POU-domain protein that inhibits neuron-specific gene activation.

A novel, structurally distinct POU-domain protein has been identified that inhibits activation by another positive POU-domain regulator of neuron-specific transcription units. Two Drosophila POU-domain proteins, I-POU and Cf1-a, are coexpressed in overlapping subsets of neurons during development. Because I-POU lacks two basic residues in the N terminus of its homeodomain, it cannot bind DNA, but it does form a stable heterodimeric complex with Cf1-a, preventing Cf1-a from binding to DNA recognition elements and from transactivating the dopa-decarboxylase gene. The inhibition by I-POU provides a potential strategy by which the activation of genes in development is controlled by a homeodomain-containing protein that does not bind DNA.

Amino Acid Sequence↗
PubMed1994

Interaction between two homeodomain proteins is specified by a short C-terminal tail.

Two yeast homeodomain proteins, a1 and alpha 2, interact and cooperatively bind the haploid-specific gene (hsg) operator, resulting in the repression of a set of genes involved in the determination of cell type. The cooperative binding of a1 and alpha 2 to DNA can be reconstituted in vitro using purified fragments of a1 and alpha 2. Only the homeodomain is needed for a1, but for alpha 2 a C-terminal 22-amino-acid tail is required as well. As most of the specificity of DNA binding appears to derive from a1, we proposed that alpha 2 functions in the a1/alpha 2 heterodimer to contact a1 with its tail. By construction and analysis of several chimaeric proteins, we investigate how two DNA-binding proteins, one with low intrinsic specificity (alpha 2) and one with no apparent intrinsic DNA-binding ability (a1), can together create a highly specific DNA-binding activity. We show that the 22-amino-acid region of alpha 2 immediately C-terminal to the homeodomain, when grafted onto the a1 homeodomain, converts a1 to a strong DNA-binding protein. This alpha 2 tail can also be attached to the Drosophila engrailed homeodomain, and the chimaeric protein now binds cooperatively to DNA with a1, showing how a simple change can create a new homeodomain combination that specifically recognizes a new DNA operator.

Animals↗
PubMed1997

Evolutionary origin of insect wings from ancestral gills.

Two hypotheses have been proposed for the origin of insect wings. One holds that wings evolved by modification of limb branches that were already present in multibranched ancestral appendages and probably functioned as gills. The second proposes that wings arose as novel outgrowths of the body wall, not directly related to any pre-existing limbs. If wings derive from dorsal structures of multibranched appendages, we expect that some of their distinctive features will have been built on genetic functions that were already present in the structural progenitors of insect wings, and in homologous structures of other arthropod limbs. We have isolated crustacean homologues of two genes that have wing-specific functions in insects, pdm (nubbin) and apterous. Their expression patterns support the hypothesis that insect wings evolved from gill-like appendages that were already present in the aquatic ancestors of both crustaceans and insects.

Amino Acid Sequence↗
PubMed2007

Identification of tightly regulated groups of genes during Drosophila melanogaster embryogenesis.

Time-series analysis of whole-genome expression data during Drosophila melanogaster development indicates that up to 86% of its genes change their relative transcript level during embryogenesis. By applying conservative filtering criteria and requiring 'sharp' transcript changes, we identified 1534 maternal genes, 792 transient zygotic genes, and 1053 genes whose transcript levels increase during embryogenesis. Each of these three categories is dominated by groups of genes where all transcript levels increase and/or decrease at similar times, suggesting a common mode of regulation. For example, 34% of the transiently expressed genes fall into three groups, with increased transcript levels between 2.5-12, 11-20, and 15-20 h of development, respectively. We highlight common and distinctive functional features of these expression groups and identify a coupling between downregulation of transcript levels and targeted protein degradation. By mapping the groups to the protein network, we also predict and experimentally confirm new functional associations.

Analysis of Variance↗
PubMed2000

Spatial, a gene expressed in thymic stromal cells, depends on three-dimensional thymus organization for its expression.

Although the importance of thymic stroma in thymopoiesis has been recognized, the underlying molecular details regarding stromal cell biology remain obscure. To study this area, we have cloned genes expressed in thymic stromal cells. Spatial is alternatively spliced to generate two mRNAs in thymus and lymph node (LN) but it is not expressed in the spleen. In mouse embryos, the short form begins expression at day 10 while the long form is not detected until day 12. Both mRNAs encode proline rich proteins and their closest homology is to homeobox and POU domain transcription factors. Spatial is not expressed in thymocytes, but it is expressed in 2-deoxyguanosine-treated day 14 fetal thymic organ culture (FTOC) and in reaggregated FTOC. These data suggest that a normal three-dimensional organization of stromal cells is required for Spatial expression. An antiserum raised against a C-terminal peptide detected proteins of 38 and 32 kDa in Western blots of total thymus proteins. In frozen thymus sections, subcapsular epithelial cells were stained with the anti-Spatial antiserum. Paracortical subcapsular cells of unknown function were also stained in the LN. Both forms of Spatial fused to the green fluorescent protein (GFP) localize to the nucleus in transfected cells.

5' Untranslated Regions↗
PubMed2003

Combined pituitary hormone deficiency in Australian children: clinical and genetic correlates.

OBJECTIVE: Mutations in the gene for the POU domain transcription factor POU1F1 (human Pit-1) have been reported in patients with GH, TSH and PRL deficiencies. PROP1 (Prophet of Pit-1) gene mutations also cause gonadotrophin deficiencies and in some cases partial ACTH deficiency. This study analyses the POU1F1 and PROP1 genes in a cohort of Australian children with combined pituitary hormone deficiency (CPHD) and correlates results with patient phenotype. PATIENTS AND DESIGN: Genomic analysis was carried out on 33 patients with CPHD referred from centres around Australia. Clinical data were collected from medical records and referring physicans. RESULTS: POU1F1 mutations were identified in two of four patients with a suggestive phenotype. In a female patient, novel compound heterozygous POU1F1 mutations were identified: Arg143Leu in exon 3 and Leu194Gln in exon 4. This patient presented with failure to thrive at 6 weeks of age and has deficiencies of TSH and GH. A previously described heterozygous Arg271Trp mutation in exon 6 of the POU1F1 gene was identified in a female infant who presented with growth failure and was diagnosed with TSH then GH deficiencies. No PROP1 mutations were identified; however, we describe a number of previously unreported PROP1 polymorphisms. No patients presenting with deficiencies of all anterior pituitary hormones early in life had POU1F1 or PROP1 gene mutations. CONCLUSIONS: In 33 Australian children with CPHD we have identified POU1F1 mutations in two patients and no PROP1 mutations. We speculate that in the majority of children other genes must be responsible for the CPHD phenotype.

Adolescent↗
PubMed2004

B cell development and immunoglobulin transcription in Oct-1-deficient mice.

The POU domain transcription factors Oct-1 and Oct-2 interact with the octamer element, a motif conserved within Ig promoters and enhancers, and mediate transcription from the Ig loci. Inactivation of Oct-2 by gene targeting results in normal B cell development and Ig transcription. To study the role of Oct-1 in these processes, the lymphoid compartment of RAG-1(-/-) animals was reconstituted with Oct-1-deficient fetal liver hematopoietic cells. Recipient mice develop B cells with levels of surface Ig expression comparable with wild type, although at slightly reduced numbers. These B cells transcribe Ig normally, respond to antigenic stimulation, undergo class switching, and use a normal repertoire of light chain variable segments. However, recipient mice show slight reductions in serum IgM and IgA. Thus, the Oct-1 protein is dispensable for B cell development and Ig transcription.

Adoptive Transfer↗
PubMed1992

RHS2, a POU domain-containing gene, and its expression in developing and adult rat.

Gene expression within the central nervous system is regulated by complex interactions of DNA-binding proteins, among which are the POU domain-containing proteins, which are distantly related to homeobox proteins. These POU domain-containing proteins have been implicated in control of transcription and replication within the central nervous system. We used degenerate primers with the PCR to isolate another POU domain-containing cDNA, RHS2, from hypothalamic RNA. Isolation of a putative full-length cDNA was accomplished by using serial dilutions of a hypothalamic cDNA library grown on solid medium. This member of the class III POU family is expressed in rats from embryonic day 11.5 into adulthood, being especially prominent in the brain. We performed double-labeling hybridization histochemistry and determined that RHS2 is coexpressed with a variety of neuropeptides in medium-sized neurons in the caudate putamen and with dynorphin in the paraventricular and supraoptic nuclei of the hypothalamus. Expression of RHS2 in the caudate putamen was increased by elimination of its nigrostriatal dopaminergic innervation.

Aging↗