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  • 1. Leipus, Arunas
    et al.
    Olsson, Ida
    Stockholms universitet.
    Berrez, Jean-Marc
    Hultenby, Kjell
    Östlund, Cecilia
    Mutvei, Ann
    Södertörn University, School of Life Sciences, Biology.
    Cwh43 is an evolutionary conserved polytopic inner nuclear membrane proteinManuscript (preprint) (Other academic)
  • 2.
    Olsson, Ida
    Södertörn University, School of Life Sciences. Stockholms universitet, Institutionen för biokemi och biofysik.
    Functional studies of nuclear envelope-associated proteins in Saccharomyces cerevisiae2008Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Proteins of the nuclear envelope play important roles in a variety of cellular processes e.g. transport of proteins between the nucleus and cytoplasm, co-ordination of nuclear and cytoplasmic events, anchoring of chromatin to the nuclear periphery and regulation of transcription. Defects in proteins of the nuclear envelope and the nuclear pore complexes have been related to a number of human diseases. To understand the cellular functions in which nuclear envelope proteins participate it is crucial to map the functions of these proteins.

    The present study was done in order to characterize the role of three different proteins in functions related to the nuclear envelope in the yeast Saccharomyces cerevisiae. The arginine methyltransferase Rmt2 was demonstrated to associate with proteins of the nuclear pore complexes and to influence nuclear export. In addition, Rmt2 was found to interact with the Lsm4 protein involved in RNA degradation, splicing and ribosome biosynthesis. These results provide support for a role of Rmt2 at the nuclear periphery and potentially in nuclear transport and RNA processing. The integral membrane protein Cwh43 was localized to the inner nuclear membrane and was also found at the nucleolus. A nuclear function for Cwh43 was demonstrated by its ability to bind DNA in vitro. A link to nucleolar functions was demonstrated by genetic analysis. Furthermore, Cwh43 is interacting with signalling pathways perhaps acting as a sensor for signals transmitted from the cytoplasm to the nucleus. The Myr1 protein was found to be membrane-associated and to interact with proteins involved in vesicular traffic. Overexpression of Myr1 affects nuclear morphology and nuclear pore distribution suggesting a function in membrane dynamics.

    In conclusion, the presented results aid in a deeper understanding of functions related to the nuclear envelope in revealing a novel link between arginine methylation and the nuclear periphery, identifying a novel inner nuclear membrane protein and a new membrane-associated protein.

  • 3.
    Olsson, Ida
    et al.
    Södertörn University, School of Life Sciences.
    Berrez, Jean-Marc
    Södertörn University, School of Life Sciences.
    Leipus, Arunas
    CHORI, Children's Hospital Oakland Research Institute, Oakland, USA / Umeå University.
    Östlund, Cecilia
    Columbia University, New York, USA.
    Mutvei, Ann
    Södertörn University, School of Life Sciences.
    The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup1002007In: Experimental Cell Research, ISSN 0014-4827, E-ISSN 1090-2422, Vol. 313, no 9, p. 1778-1789Article in journal (Refereed)
    Abstract [en]

    Arginine methylation is a post-translational modification of proteins implicated in RNA processing, protein compartmentalization, signal transduction, transcriptional regulation and DNA repair. In a screen for proteins associated with the nuclear envelope in the yeast Saccharomyces cerevisiae, we have identified the arginine methyltransferase Rmt2, previously shown to methylate the ribosomal protein L12. By indirect immunofluorescence and subcellular fractionations we demonstrate here that Rmt2 has nuclear and cytoplasmic localizations. Biochemical analysis of a fraction enriched in nuclei reveals that nuclear Rmt2 is resistant to extractions with salt and detergent, indicating an association with structural components. This was supported by affinity purification experiments with TAP-tagged Rmt2. Rmt2 was found to co-purify with the nucleoporins Nup49, Nup57 and Nup100, revealing a novel link between arginine methyltransferases and the nuclear pore complex. In addition, a genome-wide transcription study of the rmt2 Delta mutant shows significant downregulation of the transcription of MYO1, encoding the Type II myosin heavy chain required for cytokinesis and cell separation.

  • 4.
    Olsson, Ida
    et al.
    Stockholms universitet.
    Mutvei, Ann
    Södertörn University, School of Life Sciences, Biology.
    The arginine methyltransferase Rmt2 specifically associates with FG-nucleoporins – implications for a function in nuclear transportManuscript (preprint) (Other academic)
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