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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Development genes and evolution 185 (1978), S. 271-292 
    ISSN: 1432-041X
    Keywords: Homeotic mutations ; Imaginal disc ; Positional Information ; Drosophila
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations of the bithorax complex result in segmental transformations in the thorax and abdomen ofDrosophila. The haltere discs from larvae homozygous forbx 3 orpbx are transformed so that the discs contain cells that will produce wing cuticle as well as cells that produce haltere cuticle. The pattern regulation behavior of these discs has been examined. The fate maps of the two discs were established, and then the regulative behavior of a number of fragments from both types of mutant discs was established by culturing the fragments in vivo prior to metamorphosis. The most important conclusion from this work is that the cells producing, haltere cuticle and wing cuticle within the same disc share the same positional information and that they communicate during pattern regulation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 338 (1989), S. 263-264 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The fz locus was cloned by transposon tagging4'5 and fz complementary DNA clones isolated6 (the detailed molecular analysis of the fz locus will be presented elsewhere). A single 4 kilobase (kb) hybridization band is seen when northern blots of poly(A)+ pupal RNA are probed with cDNA sequences, ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 329 (1987), S. 549-551 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The bristles and hairs (and other structures) that decorate the cuticle define a tissue polarity, and have been used as an indicator of fundamental cell polarity3"7. Bristles (four-cell sensory organs) and hairs (cellular extensions that later become sclerotinized) usually point distally on ...
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] It is clear that some Pc-G genes are pleiotropic regulatory genes. Mutations in Psc can cause segmental transformations7, ventral toward dorsal transformations8, abnormal axon outgrowth in the embryonic central nervous system (CNS) (D. Smouse, N. Perrimon and C.-t Wu, personal communication) and ...
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The ability of a chimeric HP1-Polycomb (Pc) protein to bind both to heterochromatin and to euchromatic sites of Pc protein binding was exploited to detect stable protein-protein interactions in vivo. Previously, we showed that endogenous Pc protein was recruited to ectopic heterochromatic binding sites by the chimeric protein. Here, we examine the association of other Pc group (Pc-G) proteins. We show that Posterior sex combs (Psc) protein also is recruited to heterochromatin by the chimeric protein, demonstrating that Psc protein participates in direct protein-protein interaction with Pc protein or Pc-associated protein. In flies carrying temperature-sensitive alleles of Enhancer of zeste[E(z)] the general decondensation of polytene chromosomes that occurs at the restrictive temperature is associated with loss of binding of endogenous Pc and chimeric HP1-Polycomb protein to euchromatin, but binding of HP1 and chimeric HP1-Polycomb protein to the heterochromatin is maintained. The E(z) mutation also results in the loss of chimera-dependent binding to heterochromatin by endogenous Pc and Psc proteins at the restrictive temperature, suggesting that interaction of these proteins is mediated by E(z) protein. A myc-tagged full-length Suppressor 2 of zeste [Su(z)2] protein interacts poorly or not at all with ectopic Pc-G complexes, but a truncated Su(z)2 protein is strongly recruited to all sites of chimeric protein binding. Trithorax protein is not recruited to the heterochromatin by the chimeric HP1-Polycomb protein, suggesting either that this protein does not interact directly with Pc-G complexes or that such interactions are regulated. Ectopic binding of chimeric chromosomal proteins provides a useful tool for distinguishing specific protein-protein interactions from specific protein-DNA interactions important for complex assembly in vivo.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The ability of a chimeric HP1-Polycomb (Pc) protein to bind both to heterochromatin and to euchromatic sites of Pc protein binding was exploited to detect stable protein-protein interactions in vivo. Previously, we showed that endogenous Pc protein was recruited to ectopic heterochromatic binding sites by the chimeric protein. Here, we examine the association of other Pc group (Pc-G) proteins. We show that Posterior sex combs (Psc) protein also is recruited to heterochromatin by the chimeric protein, demonstrating that Psc protein participates in direct protein-protein interaction with Pc protein or Pc-associated protein. In flies carrying temperature-sensitive alleles of Enhancer of zeste[E(z)] the general decondensation of polytene chromosomes that occurs at the restrictive temperature is associated with loss of binding of endogenous Pc and chimeric HP1-Polycomb protein to euchromatin, but binding of HP1 and chimeric HP1-Polycomb protein to the heterochromatin is maintained. The E(z) mutation also results in the loss of chimera-dependent binding to heterochromatin by endogenous Pc and Psc proteins at the restrictive temperature, suggesting that interaction of these proteins is mediated by E(z) protein. A myc-tagged full-length Suppressor 2 of zeste [Su(z)2] protein interacts poorly or not at all with ectopic Pc-G complexes, but a truncated Su(z)2 protein is strongly recruited to all sites of chimeric protein binding. Trithorax protein is not recruited to the heterochromatin by the chimeric HP1-Polycomb protein, suggesting either that this protein does not interact directly with Pc-G complexes or that such interactions are regulated. Ectopic binding of chimeric chromosomal proteins provides a useful tool for distinguishing specific protein-protein interactions from specific protein-DNA interactions important for complex assembly in vivo.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The related Drosophila Suppressor 2 of zeste [Su(z)2] and Posterior sex combs (Psc) proteins are both locus-specific chromosome binding proteins. They are found at many of the same polytene chromosome loci as other Polycomb-group proteins. The 1,365 amino acid Su(z)2 protein and the 1,603 amino acid Psc protein share a conserved 200 amino acid domain, the homology region (HR). To identify the protein domain responsible for locus-specific chromosome binding, we made a series of Hsp70:cDNA deletion constructs of the Sz(z)2 gene and transformed these into flies. We found that the HR is necessary and sufficient for Su(z)2 locus-specific polytene chromosome binding. The murine Bmi-1 protein also shares the conserved HR domain. When expressed in flies, the Bmi-1 protein showed a locus-specific chromosome binding pattern similar to that of the Su(z)2 and Psc proteins. These results argue that a locus-specific chromosome binding function resides in the HR domain. Other results show that a second, low affinity, non-specific chromosome binding function is localized outside the HR in the Su(z)2 protein, and that the Su(z)2 protein contains at least two nuclear localization signals.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 12 (1991), S. 349-361 
    ISSN: 0192-253X
    Keywords: Drosophila ; Psc gene ; polycomb group gene ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The Posterior Sex Combs (Psc) gene of Drosophila is a member of the Polycomb (Pc) group of transregulatory genes. Previous analyses of the function of this gene in Drosophila em-bryogenesis have been hampered by the lack of a null mutation. We recently isolated a mutation that deletes the 5′ end of the Psc gene. This allele appears to be a null mutation, and we have used it to determine the Psc zygotic null phenotype and to look at the interactions of a null allele of Psc with five other Pc group mutations. We find evidence for transformations along both the anterior-posterior and dorsal-ventral axes in embryos of a variety of genotypes that include a null mutation in Psc. The phenotypes of embryos that are doubly mutant for a null allele of Psc and a mutation in a second Pc group gene show dramatic synergistic effects, but in their specifics they are dependent on the identify of the second Pc group gene. This is different from the relatively uniform phenotypes seen among double mutants that contained the allele Psc1, which has both gain and loss of function properties. The differences in the phenotypes of the doubly mutant embryos allow us to eliminate one class of molecular models to explain the dramatic synergism seen with mutations in this group of genes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 10 (1989), S. 249-260 
    ISSN: 0192-253X
    Keywords: Regulatory genes ; Pc group ; Drosophila embryogenesis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A wide variety of gain of function mutations have been induced in the Posterior Sex Comb (Psc) - Aristapedioid (Arp) - Suppressor 2 of zests(Su(z)2) region of the second chromosome of Drosophila. This region contains at least three apparently related genes, two of which we have been studying. Psc1 has previously been used to identify Psc as a Pc group gene; however, it is a complex mutation with both gain and loss of function character. We report here that the Pc group character of Psc is not due to a gain of function and presumably reflects the function of the wild-type gene. We also provide evidence for a maternal function for Psc, as well as the neighboring Su(z)2 gene.Su(z)2 does not appear to be a Pc group gene as it does not act in a synergistic fashion with other PC group genes in promoting posteriorly directed transformations. However, we have found that mutations in Su(z)2 do interact in a variety of interesting ways with mutations in Pc group genes.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 8 (1987), S. 99-119 
    ISSN: 0192-253X
    Keywords: Drosophila ; tissue polarity ; frizzled ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The epidermis of Drosophila has a tissue polarity that is manifested by a parallel array of polarized structures (primarily hairs and bristles). The production of normal tissue polarity requires the function of the frizzled (fz) locus. We have isolated a large number of alleles at this locus and have phenotypically characterized more than 25 of them. We have found extensive allelic variation that a previous study failed to detect. Most of the alleles fall into a hypomorphic to amorphic series. Two alleles, however, have unusual properties. These alleles, which in general are moderately strong alleles, fail to produce a rough eye phenotype that is characteristic of all the other moderate or strong fz alleles. Thus, these two alleles are tissue specific in effect. Furthermore, these two alleles also have a neomorphic or antimorphic effect on hair polarity in one region of the wing.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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