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Yeast. 1997 Jan;13(1):9-20.

The C-terminal domain of Snf3p is sufficient to complement the growth defect of snf3 null mutations in Saccharomyces cerevisiae: SNF3 functions in glucose recognition.

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1
Department of Viticulture and Enology, University of California, Davis 95616-8749, USA.

Abstract

The SNF3 protein, Snf3p, of Saccharomyces cerevisiae was initially thought to be a high affinity glucose transporter required for efficient catabolism of low glucose concentrations. We now report evidence suggesting that Snf3p is a regulatory protein and not a catabolic transporter. The C-terminal domain of Snf3p is able to complement the growth defect on solid media of snf3 null mutants independent of attachment to the membrane-spanning domains. However, the C-terminal domain is unable to fully restore high affinity glucose transport to a snf3 null strain. Examination of deletions of the C-terminal domain of intact SNF3 demonstrates that this region is required for both the growth and transport functions of Snf3p. Loss of the SNF3 gene leads to a long-term adaptation phenotype for cells grown in liquid medium at low substrate concentrations in the presence of the respiratory inhibitor, antimycin A. The presence of the C-terminal domain shortens the time required for adaptation in a snf3 null strain. Thus, Snf3p appears to affect ability to adapt to low substrate conditions, but does not confer an absolute defect in uptake of substrate. Taken together, these data suggest that Snf3p is a regulatory protein likely functioning in the detection of glucose.

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