| Autor: |
Bell, Walter, Klaassen, Paul, Ohnacker, Martin, Boller, Thomas, Herweijer, Marga, Schoppink, Peter, Van Der Zee, Peter, Wiemken, Andres |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 11/1/92, Vol. 209 Issue 3, p951-959, 9p |
| Abstrakt: |
Trehalose-6-phosphate synthase is the key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells of yeast. This enzyme was purified from a strain of Saccharomyces cerevisiae lacking vacuolar proteases. It was found to be a multimeric protein of 630 kDa. Monoclonal antibodies were raised against its smallest subunit (56 kDa) and used for screening a yeast cDNA library. This yielded an immunopositive cDNA clone of 1.7 kb, containing an open reading frame of 1485 base pairs. Its sequence, called TPSI (for trehalose-6-phosphate synthase), was represented by a single gene in the yeast genome and was found to be almost identical with the recently sequenced CIFI, a gene important for carbon catabolite inactivation, believed to be allelic with FDPI. A mutant obtained by disruption of TPS1 had a very low activity of trehalose-6-phosphate synthase, indicating that TPS1 is an important component of the enzyme. The mutant also showed a growth defect when transferred from glycerol to glucose, a phenotype similar to that of the cif1 and fdp1 mutants deficient in carbon catabolite inactivation. Thus, the smallest subunit of the biosynthetic enzyme trehalose-6- phosphate synthase appears to have, in addition, a central regulatory role in the carbohydrate metabolism of yeast. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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