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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.
Eur J Biochem. 1992 Nov 01; 209(3):951-9.EJ

Abstract

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 TPS1 (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 CIF1, a gene important for carbon catabolite inactivation, believed to be allelic with FDP1. 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.

Authors+Show Affiliations

Botanisches Institut, Universität Basel, Switzerland.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

1425702

Citation

Bell, W, et al. "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." European Journal of Biochemistry, vol. 209, no. 3, 1992, pp. 951-9.
Bell W, Klaassen P, Ohnacker M, et al. 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. Eur J Biochem. 1992;209(3):951-9.
Bell, W., Klaassen, P., Ohnacker, M., Boller, T., Herweijer, M., Schoppink, P., Van der Zee, P., & Wiemken, A. (1992). 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. European Journal of Biochemistry, 209(3), 951-9.
Bell W, et al. 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. Eur J Biochem. 1992 Nov 1;209(3):951-9. PubMed PMID: 1425702.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - 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. AU - Bell,W, AU - Klaassen,P, AU - Ohnacker,M, AU - Boller,T, AU - Herweijer,M, AU - Schoppink,P, AU - Van der Zee,P, AU - Wiemken,A, PY - 1992/11/1/pubmed PY - 1992/11/1/medline PY - 1992/11/1/entrez SP - 951 EP - 9 JF - European journal of biochemistry JO - Eur. J. Biochem. VL - 209 IS - 3 N2 - 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 TPS1 (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 CIF1, a gene important for carbon catabolite inactivation, believed to be allelic with FDP1. 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. SN - 0014-2956 UR - https://www.unboundmedicine.com/medline/citation/1425702/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_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0014-2956&date=1992&volume=209&issue=3&spage=951 DB - PRIME DP - Unbound Medicine ER -