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  • 1. Blacque, O E
    et al.
    Perens, E A
    Boroevich, K A
    Inglis, P N
    Li, C M
    Warner, A
    Khattra, J
    Holt, R A
    Ou, G S
    Mah, A K
    McKay, S J
    Huang, P
    Swoboda, Peter
    Södertörn University, School of Life Sciences. Karolinska Institute.
    Jones, S J M
    Marra, M A
    Baillie, D L
    Moerman, D G
    Shaham, S
    Leroux, M R
    Functional genomics of the cilium, a sensory organelle2005In: Current Biology, ISSN 0960-9822, E-ISSN 1879-0445, Vol. 15, no 10, p. 935-941Article in journal (Refereed)
    Abstract [en]

    Cilia and flagella play important roles in many physiological processes, including cell and fluid movement, sensory perception, and development [1]. The biogenesis and maintenance of cilia depend on intraflagellar transport (IFT), a motility process that operates bidirectionally along the ciliary axoneme [1, 2]. Disruption in IFT and cilia function causes several human disorders, including polycystic kidneys, retinal dystrophy, neurosensory impairment, and Bardet-Bledl syndrome (BBS) [3-5]. To uncover new ciliary components, including IFT proteins, we compared C. elegans ciliated neuronal and nonciliated cells through serial analysis of gene expression (SAGE) and screened for genes potentially regulated by the cillogenic transcription factor, DAF-19 [6]. Using these complementary approaches, we identified numerous candidate ciliary genes and confirmed the ciliated-cell-specific expression of 14 novel genes. One of these, C27H5.7a, encodes a ciliary protein that undergoes IFT. As with other IFT proteins, its ciliary localization and transport is disrupted by mutations in IFT and bbs genes. Furthermore, we demonstrate that the ciliary structural defect of C. elegans dyf-13(mn396) mutants is caused by a mutation in C27H5.7a. Together, our findings help define a ciliary transcriptome and suggest that DYF-13, an evolutionarily conserved protein, is a novel core IFT component required for cilia function.

  • 2.
    Gallio, Marco
    et al.
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Kylsten, Per
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Providencia may help find a function for a novel, widespread protein family2000In: Current Biology, ISSN 0960-9822, E-ISSN 1879-0445, Vol. 10, no 19, p. R693-R694Article in journal (Refereed)
  • 3. Lejeune, Erwan
    et al.
    Bortfeld, Miriam
    White, Sharon A.
    Pidoux, Alison L.
    Ekwall, Karl
    Södertörn University, School of Life Sciences. Karolinska Institute.
    Allshire, Robin C.
    Ladurner, Andreas G.
    The chromatin-remodeling factor FACT contributes to centromeric heterochromatin independently of RNAi2007In: Current Biology, ISSN 0960-9822, E-ISSN 1879-0445, Vol. 17, no 14, p. 1219-1224Article in journal (Refereed)
    Abstract [en]

    Centromeres exert vital cellular functions in mitosis and meiosis. A specialized histone and other chromatin-bound factors nucleate a dynamic protein assembly that is required for the proper segregation of sister chromatids. In several organisms, including the fission yeast, Schizosaccharomyces pombe, the RNAi pathway contributes to the formation of silent chromatin in pericentromeric regions. Little is known about how chromatin-remodeling factors contribute to heterochromatic integrity and centromere function. Here we show that the histone chaperone and remodeling complex FACT is required for centromeric-heterochromatin integrity and accurate chromosome segregation. We show that Spt16 and Pob3 are two subunits of the S. pombe FACT complex. Surprisingly, yeast strains deleted for pob3+ are viable and alleviate gene silencing at centromeric repeats and at the silent mating-type locus. Importantly, like heterochromatin and RNAi pathway mutants, Pob3 null strains exhibit lagging chromosomes on anaphase spindles. Whereas the processing of centromeric RNA transcripts into siRNAs is maintained in Pob3 mutants, Swi6-association with the centromere is reduced. Our studies provide the first experimental evidence for a role of the RNA polymerase II cofactor FACT in heterochromatin integrity and in centromere function.

  • 4. Scherfer, C
    et al.
    Karlsson, C
    Loseva, O
    Bidla, G
    Goto, A
    Havemann, J
    Dushay, Mitchell S
    Södertörn University, School of Chemistry, Biology, Geography and Environmental Science.
    Theopold, U
    Isolation and characterization of hemolymph clotting factors in Drosophila melanogaster by a pullout method2004In: Current Biology, ISSN 0960-9822, E-ISSN 1879-0445, Vol. 14, no 7, p. 625-629Article in journal (Refereed)
    Abstract [en]

    Clotting is critical in limiting loss of hemolymph and initiating wound healing in insects as well as in vertebrates [1]. Clotting is also an important immune defense, quickly forming a secondary barrier to infection, thereby immobilizing, and possibly killing bacteria directly [2, 3]. Here, we describe methods to assess clotting and to extract the clot from Drosophila larval hemolymph by using aggregation of paramagnetic beads. The validity of the assay was demonstrated by characterization of mutants. We show that clotting occurs in the absence of phenoloxidase and that the Drosophila clot binds bacteria. We also describe a pullout assay to purify the clot as a whole, free from entrapped hemocytes and cellular debris. Proteins subsequently identified by mass spectrometry include both predicted and novel clot proteins. Immune induction has been shown for three of the latter, namely Tiggrin and two unknown proteins (GC15825 and CG15293) [4,5] that we now propose function in hemolymph clotting. The most abundant clot protein is Hemolectin [6], and we confirm that hemolectin mutant larvae show clotting defects.

  • 5.
    Silverstein, Rebecka A.
    et al.
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Richardson, W
    Levin, H
    Allshire, R
    Ekwall, Karl
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    A new role for the transcriptional corepressor SIN3; Regulation of centromeres2003In: Current Biology, ISSN 0960-9822, E-ISSN 1879-0445, Vol. 13, no 1, p. 68-72Article in journal (Refereed)
    Abstract [en]

    Centromeres play a vital role in maintaining the genomic stability of eukaryotes by coordinating the equal distribution of chromosomes to daughter cells during mitosis and meiosis. Fission yeast (S. pombe) centromeres consist of a 4-9 kb central core region and 30-100 kb of flanking inner (imr/B) and outer (otr/K) repeats [1-3]. These sequences direct a laminar kinetochore structure similar to that of human centromeres [4, 5]. Centromeric heterochromatin is generally underacetylated [6, 7]. We have previously shown that inhibition of histone deacetylases (HDACs) caused hyperacetylation of centromeres and defective chromosome segregation [8]. SIN3 is a HDAC corepressor that has the ability to mediate HDAC targeting in the repression of promoters. In this study, we have characterized S. pombe sin three corepressors (Pst1p and Pst2p) to investigate whether SIN3-HDAC is required in the regulation of centromeres. We show that only pst1-1 and not pst2Delta cells displayed anaphase defects and thiabendazole sensitivity. pst1-1 cells showed reduced centromeric silencing, increased histone acetylation in centromeric chromatin, and defective centromeric sister chromatid cohesion. The HDAC Clr6p and Pst1p coimmunoprecipitated, and Pst1p colocalized with centromeres, particularly in binucleate cells. These data are consistent with a model in which Pst1 pClr6p temporally associate with centromeres to carry out the initial deacetylation necessary for subsequent steps in heterochromatin formation.

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