Identification of an asymmetrically localized determinant, Ash1p, required for lineage-specific transcription of the yeast HO gene

Article Abstract:

A mutation in the ASH1 gene of yeast cells allows daughter cells to express the HO endonuclease protein that enables them to switch mating type. This switching is typically expressed only in mother cells. The mutation comes in the form of a deletion in the daughter cell, which removes the repression on the HO gene, or overexpression in the mother cell, in which the expression of HO is prevented. These functions of the ASH1 gene points to its role in cell fate in daughter cells.

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Asymmetric accumulation of Ash1p in postanaphase nuclei depends on a myosin and restricts mating-type switching to mother cells

Article Abstract:

The gene Ash1 is expressed in yeast cells that have newly budded off from the mother cell and is responsible for preventing the expression of HO endonuclease. Ash1 produces a zinc finger protein that accumulates in the daughter cell nucleus after the anaphase stage of budding. The zinc finger protein requires the presence of She1p and Myo4p myosin proteins, which are abundant in the daughter cell. Thus, Ash1 accumulates and restricts HO expression in the daughter cell.

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Localization of Bud2p, a GTPase-activating protein necessary for programming cell polarity in yeast to the presumptive bud site

Article Abstract:

Bud2 protein, a protein that activates GTPase and that is required for programming cell polarity in yeast to the presumed bud site, and its localization are discussed. It appears that Bud2p localization is not dependent on Bud1p, depending instead on integrity of the septins, and that it is positioned in G(sub.1) cells by recognizing cell type-specific landmarks at the likely bud site

United States, Statistical Data Included, Cellular signal transduction, Allosteric proteins

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