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  • 1. Dunleavy, Elaine M.
    et al.
    Pidoux, Alison L.
    Monet, Marie
    Bonilla, Carolina
    Richardson, William
    Hamilton, Georgina L.
    Ekwall, Karl
    Södertörn University, School of Life Sciences. Karolinska Institute.
    McLaughlin, Paul J.
    Allshire, Robin C.
    A NASP (N1/N2)-related protein, Sim3, binds CENP-A and is required for its deposition at fission yeast Centromeres2007In: Molecular Cell, ISSN 1097-2765, E-ISSN 1097-4164, Vol. 28, no 6, p. 1029-1044Article in journal (Refereed)
    Abstract [en]

    A defining feature of centromeres is the presence of the histone H3 variant CENP-A(Cnp1). It is not known how CENP-A(Cnp1) is specifically delivered to, and assembled into, centromeric chromatin. Through a screen for factors involved in kinetochore integrity in fission yeast, we identified Sim3. Sim3 is homologous to known histone binding proteins NASP(Human) and N1/N2(Xenopus) and aligns with Hif1(S. cerevisiae), defining the SHNi-TPR family. Sim3 is distributed throughout the nucleoplasm, yet it associates with CENP-A(Cnp1) and also binds H3. Cells defective in Sim3 function have reduced levels of CENP-A(CnP1) at centromeres (and increased H3) and display chromosome segregation defects. Sim3 is required to allow newly synthesized CENP-A(Cnp1) to accumulate at centromeres in S and G2 phase-arrested cells in a replication-independent mechanism. We propose that one function of Sim3 is to act as an escort that hands off CENP-A(Cnp1) to chromatin assembly factors, allowing its incorporation into centromeric chromatin.

  • 2.
    Ekwall, Karl
    Södertörn University, School of Chemistry, Biology, Geography and Environmental Science. Karolinska Institute.
    The RITS complex - A direct link between small RNA and heterochromatin2004In: Molecular Cell, ISSN 1097-2765, E-ISSN 1097-4164, Vol. 13, no 3, p. 304-305Article in journal (Refereed)
  • 3.
    Neely, K E
    et al.
    Pennsylvania State University, Pennsylvania, USA.
    Hassan, A H
    Pennsylvania State University, Pennsylvania, USA.
    Wallberg, Annika E
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Steger, D J
    Pennsylvania State University, Pennsylvania, USA.
    Cairns, B R
    University of Utah School of Medicine, Salt Lake City, USA.
    Wright, Athony P H
    Södertörn University, Avdelning Naturvetenskap. Karolinska Institutet.
    Workman, J L
    Pennsylvania State University, Pennsylvania, USA.
    Activation domain-mediated targeting of the SWI/SNF complex to promoters stimulates transcription from nucleosome arrays1999In: Molecular Cell, ISSN 1097-2765, E-ISSN 1097-4164, Vol. 4, no 4, p. 649-655Article in journal (Refereed)
    Abstract [en]

    The yeast SWI/SNF complex is required for the transcription of several yeast genes and has been shown to alter nucleosome structure in an ATP-dependent reaction. In this study, we show that the complex stimulated in vitro transcription from nucleosome templates in an activation domain-dependent manner. Transcription stimulation by SWI/SNF required an activation domain with which it directly interacts. The acidic activation domains of VP16, Gcn4, Swi5, and Hap4 interacted directly with the purified SWI/SNF complex and with the SWI/SNF complex in whole-cell extracts. The similarity of activation domain interactions and transcriptional stimulation between SWI/SNF and the SAGA histone acetyltransferase complex may account for their apparent overlapping functions in vivo.

  • 4.
    Zhu, Xuefeng
    et al.
    Karolinska Institutet.
    Wirén, Marianna
    Södertörn University, School of Life Sciences. Karolinska Institutet.
    Sinha, Indranil
    Södertörn University, School of Life Sciences. Karolinska Institutet.
    Rasmussen, Nina N
    Institute of Molecular Biology, Copenhagen, Denmark.
    Linder, Tomas
    Karolinska Institutet.
    Holmberg, Steen
    Institute of Molecular Biology, Copenhagen, Denmark.
    Ekwall, Karl
    Södertörn University, School of Life Sciences. Karolinska Institutet.
    Gustafsson, Claes M
    Karolinska Institutet.
    Genome-wide occupancy profile of mediator and the Srb8-11 module reveals interactions with coding regions2006In: Molecular Cell, ISSN 1097-2765, E-ISSN 1097-4164, Vol. 22, no 2, p. 169-178Article in journal (Refereed)
    Abstract [en]

    Mediator exists in a free form containing the Med12, Med13, CDK8, and CycC subunits (the Srb8-11 module) and a smaller form, which lacks these four subunits and associates with RNA polymerase II (Pol II), forming a holoenzyme. We use chromatin immunoprecipitation (ChIP) and DNA microarrays to investigate genome-wide localization of Mediator and the Srb8-11 module in fission yeast. Mediator and the Srb8-11 module display similar binding patterns, and interactions with promoters and upstream activating sequences correlate with increased transcription activity. Unexpectedly, Mediator also interacts with the downstream coding region of many genes. These interactions display a negative bias for positions closer to the 5' ends of open reading frames (ORFs) and appear functionally important, because downregulation of transcription in a temperature-sensitive med17 mutant strain correlates with increased Mediator occupancy in the coding region. We propose that Mediator coordinates transcription initiation with transcriptional events in the coding region of eukaryotic genes.

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