Characterization of the 56‐kDa subunit of yeast trehalose‐6‐phosphate synthase and cloning of its gene reveal its identity with the product of CIF1, a regulator of carbon catabolite inactivation
作者： Walter BELL , Paul KLAASSEN , Martin OHNACKER , Thomas BOLLER , Marga HERWEIJER
DOI: 10.1111/J.1432-1033.1992.TB17368.X
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摘要: Trehalose-6-phosphate synthase is the key enzyme for biosynthesis of trehalose, major soluble carbohydrate in resting cells yeast. This was purified from a strain Saccharomyces cerevisiae lacking vacuolar proteases. It found to be multimeric protein 630 kDa. Monoclonal antibodies were raised against its smallest subunit (56 kDa) and used screening yeast cDNA library. yielded an immunopositive clone 1.7 kb, containing open reading frame 1485 base pairs. Its sequence, called TPS1 (for trehalose-6-phosphate synthase), represented by single gene genome almost identical with recently sequenced CIF1, important carbon catabolite inactivation, believed allelic FDP1. A mutant obtained disruption had very low activity synthase, indicating that component enzyme. The also showed growth defect when transferred glycerol glucose, phenotype similar cif1 fdp1 mutants deficient inactivation. Thus, biosynthetic appears have, addition, central regulatory role metabolism
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