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The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2007 In: Experimental Cell Research, ISSN 0014-4827, Vol. 313, no 9, 1778-1789 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2007. Vol. 313, no 9, 1778-1789 p.
URN: urn:nbn:se:su:diva-24985OAI: diva2:198660
Part of urn:nbn:se:su:diva-7599Available from: 2008-05-08 Created: 2008-05-08Bibliographically approved
In thesis
1. Functional studies of nuclear envelope-associated proteins in Saccharomyces cerevisiae
Open this publication in new window or tab >>Functional studies of nuclear envelope-associated proteins in Saccharomyces cerevisiae
2008 (English)Doctoral 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.

Place, publisher, year, edition, pages
Stockholm: Institutionen för biokemi och biofysik, 2008. 58 p.
Nucleus, nuclear envelope, nuclear pore complexes, vesicular traffic, arginine methylation, Rmt2, Cwh43, Myr1
National Category
Biochemistry and Molecular Biology
Research subject
urn:nbn:se:su:diva-7599 (URN)978-91-7155-666-0 (ISBN)
Public defence
2008-05-29, MA 636, Södertörns högskola, Alfred Nobels allé 7, Huddinge, 13:00 (English)
Available from: 2008-05-08 Created: 2008-05-08 Last updated: 2010-01-13Bibliographically approved

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