Search Results - (Author, Cooperation:W. Z. Cande)
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1Latest Papers from Table of Contents or Articles in PressStaff View
Publication Date: 2011-07-05Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Cdc20 Proteins ; Cell Cycle/genetics/physiology ; Cell Cycle Proteins/metabolism ; Chromosomal Proteins, Non-Histone/*metabolism ; Chromosomes, Fungal/chemistry/genetics/metabolism ; DNA Replication/*physiology ; Epigenesis, Genetic ; Gene Expression Regulation, Fungal ; Gene Silencing ; Heterochromatin/chemistry/genetics/metabolism ; Histones/chemistry/*metabolism ; Lysine/metabolism ; Methylation ; Multiprotein Complexes/chemistry/metabolism ; RNA Interference ; RNA Polymerase II/metabolism ; RNA, Small Interfering ; Schizosaccharomyces/cytology/*genetics/*metabolism ; Schizosaccharomyces pombe Proteins/*metabolism ; Transcription Factors/metabolism ; Transcription, GeneticPublished by: -
2Latest Papers from Table of Contents or Articles in PressM. Zaratiegui ; S. E. Castel ; D. V. Irvine ; A. Kloc ; J. Ren ; F. Li ; E. de Castro ; L. Marin ; A. Y. Chang ; D. Goto ; W. Z. Cande ; F. Antequera ; B. Arcangioli ; R. A. Martienssen
Nature Publishing Group (NPG)
Published 2011Staff ViewPublication Date: 2011-10-18Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Centromere/genetics/metabolism ; Chromosomal Proteins, Non-Histone/genetics/metabolism ; DNA Damage ; DNA Replication/*physiology ; DNA-Directed DNA Polymerase/metabolism ; *Gene Silencing ; Heterochromatin/*genetics/*metabolism ; Histones/metabolism ; Homologous Recombination ; Models, Genetic ; Molecular Sequence Data ; *RNA Interference ; RNA Polymerase II/*metabolism ; RNA, Small Interfering/genetics/metabolism ; Replication Origin ; S Phase ; Schizosaccharomyces/*genetics ; Schizosaccharomyces pombe Proteins/genetics/metabolism ; Transcription, GeneticPublished by: -
3Articles: DFG German National LicensesStaff View
ISSN: 1432-2048Source: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary By application of agar blocks (“side blocks”) against the inner and outer epidermis of maize (Zea mays L.) coleoptiles whose cuticle has been abraded it is found that radioactive auxin in the polar transport stream exchanges rapidly with the tissue's free space and therefore does not move confined within the symplast. Polar transport of IAA is demonstrable in Avena coleoptile segments plasmolyzed in 0.5 and 0.7 M mannitol, in which most of the plasmodesmatal connections between successive cells in the polar transport pathway appear to have been broken. We conclude that during polar transport IAA probably moves from cell to cell by crossing the plasmalemmas and the free space between successive cells, rather than via plasmodesmata. Auxin in the polar transport stream exchanges rapidly with side blocks by a cyanide-and azide-insensitive, presumably passive, process. A similarly passive uptake takes place into the cells from an external donor. NPA almost completely inhibits efflux from the polar transport stream even though it does not inhibit uptake; its inhibition of efflux is completely reversed by azide or cyanide. These findings are compatible either with the traditional model of polar transport as passive uptake combined with an active basal efflux pump for IAA, or with the model of purely passive polar transport driven by pH and/or potential differences across the plasma membrane, provided certain ad hoc assumptions are made about the characteristics of the IAA anion carrier that would be operating in either model.Type of Medium: Electronic ResourceURL: -
4Articles: DFG German National LicensesStaff View
ISSN: 1432-2048Source: Springer Online Journal Archives 1860-2000Topics: BiologyNotes: Summary When cytoplasmie streaming in oat and maize coleoptile cells is completely inhibited by cytochalasin B (CB), polar transport of auxin (indole-3-acetic acid) continues at a slightly reduced rate. Therefore, cytoplasmic streaming is not required for polar transport. Auxin induces elongation in CB-inhibited coleoptile and pea stem segments, but elongation rate is reduced about 40% by CB. Therefore, stimulation of cytoplasmic streaming cannot be the means by which auxin promotes cell elongation, but streaming may be beneficial to elongation growth although not essential to it. A more severe inhibition of elongation develops after several hours in CB. With coleoptiles this could be due to inhibition of sugar uptake; in pea tissue it may be due to permeability changes and cytoplasmic degeneration. CB does not disorganize or disorient microfilament bundles when it inhibits streaming in maize, but appears instead to cause hypercondensation of microfilament material.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesWordeman, L. ; Davis, F. M. ; Rao, P. N. ; Cande, W. Z.
New York, NY : Wiley-Blackwell
Published 1989Staff ViewISSN: 0886-1544Keywords: phosphorylation ; MPM-2 ; mitotic spindle ; microtubule-associated protein ; Life and Medical Sciences ; Cell & Developmental BiologySource: Wiley InterScience Backfile Collection 1832-2000Topics: BiologyMedicineNotes: Mitotic spindles isolated from the diatom Stephanopyxis turris become thiophosphorylated in the presence of ATPγS at specific locations within the mitotic apparatus, resulting in a stimulation of ATP-dependent spindle elongation in vitro. Here, using indirect immunofluorescence, we compare the staining pattern of an antibody against thiophosphorylated proteins to that of MPM-2, an antibody against mitosis-specific phosphoproteins, in isolated spindles. Both antibodies label spindle poles, kinetochores, and the midzone. Neither antibody exhibits reduced labeling in salt-extracted spindles, although prior salt extraction inhibits thiophosphorylation in ATPγS. Furthermore, both antibodies recognize a 205 kd band on immunoblots of spindle extracts. Microtubule-organizing centers and mitotic spindles label brightly with the MPM-2 antibody in intact cells. These results show that functional mitotic spindles isolated from S. turris are phosphorylated both in vivo and in vitro. We discuss the possible role of phosphorylated cytoskeletal proteins in the control of mitotic spindle function.Additional Material: 5 Ill.Type of Medium: Electronic ResourceURL: -
6Articles: DFG German National LicensesStaff View
ISSN: 0265-9247Keywords: Life and Medical Sciences ; Cell & Developmental BiologySource: Wiley InterScience Backfile Collection 1832-2000Topics: BiologyMedicineNotes: At anaphase chromosomes move to the spindle poles (anaphase A) and the spindle poles move apart (anaphase B). In vitro studies using isolated diatom spindles demonstrate that the primary mechano-chemical event responsible for spindle elongation is the sliding apart of half-spindle microtubules. Further, these forces are generated within the zone of microtubule overlap in the spindle midzone.Additional Material: 3 Ill.Type of Medium: Electronic ResourceURL: