Schizosaccharomyces pombe Snf2SR, a novel SNF2 family protein, interacts with Ran GTPase and modulates both RanGEF and RanGAP activities
Autor: | Hideo Nishitani, Takeharu Nishimoto, Tomoyuki Ohba, Hitoshi Nishijima |
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Rok vydání: | 2008 |
Předmět: |
Adenosine Triphosphatases
Cell Nucleus biology GTPase-activating protein Protein family Chromosomal Proteins Non-Histone Helicase Cell Biology biology.organism_classification Molecular biology Chromatin remodeling Cell biology Histones ran GTP-Binding Protein Schizosaccharomyces Ran Schizosaccharomyces pombe Genetics biology.protein RanGAP Schizosaccharomyces pombe Proteins Guanine nucleotide exchange factor Gene Deletion |
Zdroj: | Genes to Cells. 13:571-582 |
ISSN: | 1365-2443 1356-9597 |
DOI: | 10.1111/j.1365-2443.2008.01190.x |
Popis: | Snf2SR, a suppressor of rna1(ts), which is a temperature-sensitive mutation in Schizosaccharomyces pombe RanGAP (GTPase activating protein), possesses both the SNF2 and the helicase domains conserved in the chromatin remodeling SNF2 ATPase/helicase protein family. We have now clarified a function of Snf2SR. Snf2SR indeed showed DNA-stimulated ATPase activity, proving that it is a member of the SNF2 ATPase/helicase family. Consistent with this role, Snf2SR was localized in the nucleus and cell fractionation analysis revealed that Snf2SR was tightly associated with the nuclear matrix. The disruption of snf2SR(+) was detrimental for a cell proliferation of S. pombe. Snf2SR that did not enhance RanGAP activity by itself, but abolished histone-H3-mediated RanGAP inhibition, as previously reported for the histone H3 methyltransferase, Clr4, another rna1(ts) suppressor. In contrast to Clr4, Snf2SR directly bound to the GDP-bound form of the S. pombe Ran homologue Spi1 and enhanced the nucleotide exchange activity of Pim1, the S. pombe RanGEF (guanine nucleotide exchange factor). Over-expression of Spi1-G18V, a Ran GTPase mutant fixed in the GTP-bound form, was lethal to S. pombe Deltasnf2SR. Together, our results indicate that Snf2SR is involved in the Ran GTPase cycle in vivo. |
Databáze: | OpenAIRE |
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