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Functional studies of nuclear envelope-associated proteins in Saccharomyces cerevisiae
Södertörn University, School of Life Sciences. Stockholms universitet, Institutionen för biokemi och biofysik.
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: Department of Biochemistry and Biophysics, Stockholm university , 2008. , 58 p.
Keyword [en]
Nucleus, nuclear envelope, nuclear pore complexes, vesicular traffic, arginine methylation, Rmt2, Cwh43, Myr1
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:sh:diva-32040ISBN: 978-91-7155-666-0 (print)OAI: oai:DiVA.org:sh-32040DiVA: diva2:1073764
Public defence
2008-05-29, MA 636, Alfred Nobels allé 7, Huddinge, 13:00 (English)
Opponent
Supervisors
Available from: 2017-02-13 Created: 2017-02-13 Last updated: 2017-02-13Bibliographically approved
List of papers
1. The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100
Open this publication in new window or tab >>The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100
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2007 (English)In: Experimental Cell Research, ISSN 0014-4827, E-ISSN 1090-2422, Vol. 313, no 9, 1778-1789 p.Article in journal (Refereed) Published
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.

National Category
Cancer and Oncology Cell Biology
Identifiers
urn:nbn:se:sh:diva-14224 (URN)10.1016/j.yexcr.2007.03.007 (DOI)000246348400004 ()17448464 (PubMedID)2-s2.0-35548947153 (Scopus ID)
Available from: 2011-12-19 Created: 2011-12-19 Last updated: 2017-02-13Bibliographically approved
2. The arginine methyltransferase Rmt2 specifically associates with FG-nucleoporins – implications for a function in nuclear transport
Open this publication in new window or tab >>The arginine methyltransferase Rmt2 specifically associates with FG-nucleoporins – implications for a function in nuclear transport
(English)Manuscript (preprint) (Other academic)
National Category
Biological Sciences
Identifiers
urn:nbn:se:sh:diva-32041 (URN)
Note

Som manuskript i avhandling. As manuscript in dissertation.

Available from: 2008-05-08 Created: 2017-02-13 Last updated: 2017-02-13Bibliographically approved
3. Cwh43 is an evolutionary conserved polytopic inner nuclear membrane protein
Open this publication in new window or tab >>Cwh43 is an evolutionary conserved polytopic inner nuclear membrane protein
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(English)Manuscript (preprint) (Other academic)
National Category
Biological Sciences
Identifiers
urn:nbn:se:sh:diva-32042 (URN)
Note

Som manuskript i avhandling. As manuscript in dissertation.

Available from: 2008-05-08 Created: 2017-02-13 Last updated: 2017-02-13Bibliographically approved
4. Characterization of MYR1, a dosage suppressor of YPT6 and RIC1 deficient mutants
Open this publication in new window or tab >>Characterization of MYR1, a dosage suppressor of YPT6 and RIC1 deficient mutants
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2008 (English)In: Current Genetics, ISSN 0172-8083, E-ISSN 1432-0983, Vol. 53, no 4, 235-247 p.Article in journal (Refereed) Published
Abstract [en]

Membrane traffic is tightly regulated and the Rab protein family of small GTPases plays a central role in this regulation. One member of this family is the Saccharomyces cerevisae protein Ypt6. To search for new genes interacting with Ypt6-related pathways, we performed a genetic screen for high copy suppressors of ypt6 Delta temperature sensitivity at 35 degrees C. Among the suppressors, MYR1 was also able to suppress the temperature sensitive mutant lacking Ric1, a subunit of the Ypt6 guanine exchanging factor complex Ric1/Rgp1. Myr1 is characterized by a coiled coil region and a GYF domain, a protein module binding proline-rich sequences. Myr1 is able to bind membranes but is also associated with larger structures insoluble in Triton X-100. By immunofluorescence, Myr1 shows a network-like pattern as well as small foci. Overexpression of Myr1 influences nuclear envelope morphology and high levels are lethal. This lethality is rescued when the N-terminal region, containing the GYF domain, is deleted. The transcription profile of a myr1 Delta strain shows effects on genes involved in nuclear migration, Ras signalling and transcription. Taken together, these results suggest that Myr1 is a novel factor linked to the secretory pathway and important cellular regulatory mechanisms.

National Category
Biological Sciences
Identifiers
urn:nbn:se:sh:diva-17359 (URN)10.1007/s00294-008-0183-0 (DOI)000254182700005 ()2-s2.0-41149157331 (Scopus ID)
Available from: 2012-11-20 Created: 2012-11-19 Last updated: 2017-02-13Bibliographically approved

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