Shared control of maltose and trehalose utilization in Candida utilis

Abstract

Trehalose biosynthesis and its hydrolysis have been extensively studied in yeast, but few reports have addressed the catabolism of exogenously supplied trehalose. Here we report the catabolism of exogenous trehalose by Candida utilis. In contrast to the biphasic growth in glucose, the growth of C. utilis in a mineral medium with trehalose as the sole carbon and energy source is aerobic and exhibits the Kluyver effect. Trehalose is transported into the cell by an inducible trehalose transporter (K M of 8 mM and V MAX of 1.8 µmol trehalose min -1 mg cell (dry weight) -1 . The activity of the trehalose transporter is high in cells growing in media containing trehalose or maltose and very low or absent during the growth in glucose or glycerol. Similarly, total trehalase activity was increased from about 1.0 mU/mg protein in cells growing in glucose to 39.0 and 56.2 mU/mg protein in cells growing in maltose and trehalose, respectively. Acidic and neutral trehalase activities increased during the growth in trehalose, with neutral trehalase contributing to about 70% of the total activity. In addition to the increased activities of the trehalose transporter and trehalases, growth in trehalose promoted the increase in the activity of α-glucosidase and the maltose transporter. These results clearly indicate that maltose and trehalose promote the increase of the enzymatic activities necessary to their catabolism but are also able to stimulate each other's catabolism, as reported to occur in Escherichia coli. We show here for the first time that trehalose induces the catabolism of maltose in yeast. Correspondence

Acid trehalase in yeasts and filamentous fungi: Localization, regulation and physiological function

“…In favour of this idea was the observation that deletion of AGT1 or NTH1 dramatically increased the lag phase of growth on trehalose. Recently, Panek's group [53] presented evidence that the growth of Candida utilis on trehalose could proceed via its uptake in a concerted manner with acid and neutral trehalase. Therefore, the dual system for trehalose assimilation might exist in other yeast species and filamentous fungi.…”

Secretion of the acid trehalase encoded by the CgATH1 gene allows trehalose fermentation by Candida glabrata

“…Nevertheless, this sugar is not fermented by S. cerevisiae cells, opening new opportunities for the study of energy metabolism in yeasts (Malluta et al 2000;Jules et al 2004Jules et al , 2005Mouret et al 2006). There is evidence that in other yeasts, such as C. utilis, the uptake and intracellular hydrolysis of the disaccharide may be the major pathway for trehalose utilization (Roy and Ghosh 2001;Rolim et al 2003), while in C. albicans and C. parasilopsis an acid trehalase (encoded by the ATC1 gene) was shown to be required for growth on trehalose (Pedreno et al 2004;Sánchez-Fresneda et al, 2014).…”

Further study of theHansenula polymorpha MALlocus: characterization of the α-glucoside permease encoded by theHpMAL2gene

“…In contrast to the situation in Sa. cerevisiae , trehalose can induce its own transport in C. utilis (Rolim et al , 2003). Our data (Fig.…”

“…The pH optimum of 5.0 has also been shown for PNPG and trehalose transport in Sa. cerevisiae (Stambuk et al , 1996; Stambuk, 2000), although maltose and α‐glucoside transport in yeasts has mostly been assayed at pH 4.2–4.5 (Peinado et al , 1987; Cheng & Michels, 1991; Day et al , 2002; Rolim et al , 2003). The results of our study indicate that HpMal2p functions as a proton symporter.…”