Glucose signaling in yeast is partially mimicked by galactose and does not require the Tps1 protein.

Glucose produces multiple effects in Saccharomyces cerevisiae, as it controls the expression of many genes and the activity of various enzymes. However, the elements involved in glucose signaling are not well characterized. In this work the capacity of galactose to bring about the same effects than glucose has been assessed. Galactose mimics glucose only partially; it is suggested that it does not interact with a "sensor" in the plasma membrane and that it produces a weaker intracellular signal than glucose. To examine whether trehalose-6P synthase (Tps1) is required to transduce the glucose signal, we have constructed a tps1 hxk2/tps1 HXK2 strain which, at difference of a tps1 strain, grows on glucose, and, at difference of a tps1 hxk2 strain, still possess the Hxk2 protein, possibly involved in glucose repression. From the response of this strain to glucose, we conclude that Tps1 does not play a prominent role in glucose signaling.