sh.sePublications
Change search
Link to record
Permanent link

Direct link
Berrez, Jean-Marc
Publications (3 of 3) Show all publications
Georgiev, A., Leipus, A., Olsson, I., Berrez, J.-M. & Mutvei, A. (2008). Characterization of MYR1, a dosage suppressor of YPT6 and RIC1 deficient mutants. Current Genetics, 53(4), 235-247
Open this publication in new window or tab >>Characterization of MYR1, a dosage suppressor of YPT6 and RIC1 deficient mutants
Show others...
2008 (English)In: Current Genetics, ISSN 0172-8083, E-ISSN 1432-0983, Vol. 53, no 4, p. 235-247Article 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: 2017-12-07Bibliographically approved
Olsson, I., Berrez, J.-M., Leipus, A., Östlund, C. & Mutvei, A. (2007). The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100. Experimental Cell Research, 313(9), 1778-1789
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
Show others...
2007 (English)In: Experimental Cell Research, ISSN 0014-4827, E-ISSN 1090-2422, Vol. 313, no 9, p. 1778-1789Article 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: 2017-12-08Bibliographically approved
Leipus, A., Olsson, I., Berrez, J.-M., Hultenby, K., Östlund, C. & Mutvei, A.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
Show others...
(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
Organisations

Search in DiVA

Show all publications