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Vol. 17, Issue 4, 1768-1778, April 2006

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Yeast Nuclear Envelope Subdomains with Distinct Abilities to Resist Membrane Expansion

Joseph L. Campbell ^*, Alexander Lorenz , Keren L. Witkin ^*, Thomas Hays ^*, Josef Loidl , and Orna Cohen-Fix ^*

^* The Laboratory of Molecular and Cellular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892; Department of Chromosome Biology, University of Vienna, 1030 Vienna, Austria

Submitted September 6, 2005; Revised January 25, 2006; Accepted January 26, 2006
Monitoring Editor: Karsten Weis

Little is known about what dictates the round shape of the yeast Saccharomyces cerevisiae nucleus. In spo7 mutants, the nucleus is misshapen, exhibiting a single protrusion. The Spo7 protein is part of a phosphatase complex that represses phospholipid biosynthesis. Here, we report that the nuclear protrusion of spo7 mutants colocalizes with the nucleolus, whereas the nuclear compartment containing the bulk of the DNA is unaffected. Using strains in which the nucleolus is not intimately associated with the nuclear envelope, we show that the single nuclear protrusion of spo7 mutants is not a result of nucleolar expansion, but rather a property of the nuclear membrane. We found that in spo7 mutants the peripheral endoplasmic reticulum (ER) membrane was also expanded. Because the nuclear membrane and the ER are contiguous, this finding indicates that in spo7 mutants all ER membranes, with the exception of the membrane surrounding the bulk of the DNA, undergo expansion. Our results suggest that the nuclear envelope has distinct domains that differ in their ability to resist membrane expansion in response to increased phospholipid biosynthesis. We further propose that in budding yeast there is a mechanism, or structure, that restricts nuclear membrane expansion around the bulk of the DNA.

Abbreviations used: DAPI, 4,6-diamidino-2-phenylindole; ER, endoplasmic reticulum; FISH, fluorescence in situ hybridization; HU, hydroxyurea.

Address correspondence to: Orna Cohen-Fix (ornacf{at}helix.nih.gov).

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