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Regulation of the yeast trehalose-synthase complex by cyclic AMP-dependent phosphorylation.
Biochim Biophys Acta 2014; 1840(6):1646-50BB

Abstract

BACKGROUND

Trehalose is an important protectant in several microorganisms. In Saccharomyces cerevisiae, it is synthesized by a large complex comprising the enzymes Tps1 and Tps2 and the subunits Tps3 and Tsl1, showing an intricate metabolic control.

METHODS

To investigate how the trehalose biosynthesis pathway is regulated, we analyzed Tps1 and Tps2 activities as well as trehalose and trehalose-6-phosphate (T6P) contents by mass spectrometry.

RESULTS

Tsl1 deficiency totally abolished the increase in Tps1 activity and accumulation of trehalose in response to a heat stress, whereas absence of Tps3 only reduced Tps1 activity and trehalose synthesis. In extracts of heat stressed cells, Tps1 was inhibited by T6P and by ATP. Mg(2+) in the presence of cAMP. In contrast, cAMP-dependent phosphorylation did not inhibit Tps1 in tps3 cells, which accumulated a higher proportion of T6P after stress. Tps2 activity was not induced in a tps3 mutant.

CONCLUSION

Taken together these results suggest that Tsl1 is a decisive subunit for activity of the TPS complex since in its absence no trehalose synthesis occurred. On the other hand, Tps3 seems to be an activator of Tps2. To perform this task, Tps3 must be non-phosphorylated. To readily stop trehalose synthesis during stress recovery, Tps3 must be phosphorylated by cAMP-dependent protein kinase, decreasing Tps2 activity and, consequently, increasing the concentration of T6P which would inhibit Tps1.

GENERAL SIGNIFICANCE

A better understanding of TPS complex regulation is essential for understanding how yeast deals with stress situations and how it is able to recover when the stress is over.

Authors+Show Affiliations

Department of Biochemistry, Chemistry Institute, Federal University of Rio de Janeiro, Brazil. Electronic address: eduardotrevisol@gmail.com.Department of Biochemistry, Chemistry Institute, Federal University of Rio de Janeiro, Brazil.Department of Genetics and Molecular Biology, Bioinformatics and Computational Biology Group, Federal University of Rio de Janeiro State, Brazil.Department of Biochemistry, Chemistry Institute, Federal University of Rio de Janeiro, Brazil. Electronic address: eliscael@iq.ufrj.br.

Pub Type(s)

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

Language

eng

PubMed ID

24380875

Citation

Trevisol, Eduardo T V., et al. "Regulation of the Yeast Trehalose-synthase Complex By Cyclic AMP-dependent Phosphorylation." Biochimica Et Biophysica Acta, vol. 1840, no. 6, 2014, pp. 1646-50.
Trevisol ET, Panek AD, De Mesquita JF, et al. Regulation of the yeast trehalose-synthase complex by cyclic AMP-dependent phosphorylation. Biochim Biophys Acta. 2014;1840(6):1646-50.
Trevisol, E. T., Panek, A. D., De Mesquita, J. F., & Eleutherio, E. C. (2014). Regulation of the yeast trehalose-synthase complex by cyclic AMP-dependent phosphorylation. Biochimica Et Biophysica Acta, 1840(6), pp. 1646-50. doi:10.1016/j.bbagen.2013.12.010.
Trevisol ET, et al. Regulation of the Yeast Trehalose-synthase Complex By Cyclic AMP-dependent Phosphorylation. Biochim Biophys Acta. 2014;1840(6):1646-50. PubMed PMID: 24380875.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Regulation of the yeast trehalose-synthase complex by cyclic AMP-dependent phosphorylation. AU - Trevisol,Eduardo T V, AU - Panek,Anita D, AU - De Mesquita,Joelma F, AU - Eleutherio,Elis C A, Y1 - 2013/12/28/ PY - 2013/09/10/received PY - 2013/11/28/revised PY - 2013/12/09/accepted PY - 2014/1/2/entrez PY - 2014/1/2/pubmed PY - 2014/7/6/medline KW - Phosphorylation KW - Ras/cAPK pathway KW - Saccharomyces cerevisiae KW - Stress response KW - Trehalose SP - 1646 EP - 50 JF - Biochimica et biophysica acta JO - Biochim. Biophys. Acta VL - 1840 IS - 6 N2 - BACKGROUND: Trehalose is an important protectant in several microorganisms. In Saccharomyces cerevisiae, it is synthesized by a large complex comprising the enzymes Tps1 and Tps2 and the subunits Tps3 and Tsl1, showing an intricate metabolic control. METHODS: To investigate how the trehalose biosynthesis pathway is regulated, we analyzed Tps1 and Tps2 activities as well as trehalose and trehalose-6-phosphate (T6P) contents by mass spectrometry. RESULTS: Tsl1 deficiency totally abolished the increase in Tps1 activity and accumulation of trehalose in response to a heat stress, whereas absence of Tps3 only reduced Tps1 activity and trehalose synthesis. In extracts of heat stressed cells, Tps1 was inhibited by T6P and by ATP. Mg(2+) in the presence of cAMP. In contrast, cAMP-dependent phosphorylation did not inhibit Tps1 in tps3 cells, which accumulated a higher proportion of T6P after stress. Tps2 activity was not induced in a tps3 mutant. CONCLUSION: Taken together these results suggest that Tsl1 is a decisive subunit for activity of the TPS complex since in its absence no trehalose synthesis occurred. On the other hand, Tps3 seems to be an activator of Tps2. To perform this task, Tps3 must be non-phosphorylated. To readily stop trehalose synthesis during stress recovery, Tps3 must be phosphorylated by cAMP-dependent protein kinase, decreasing Tps2 activity and, consequently, increasing the concentration of T6P which would inhibit Tps1. GENERAL SIGNIFICANCE: A better understanding of TPS complex regulation is essential for understanding how yeast deals with stress situations and how it is able to recover when the stress is over. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/24380875/Regulation_of_the_yeast_trehalose_synthase_complex_by_cyclic_AMP_dependent_phosphorylation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0304-4165(13)00537-0 DB - PRIME DP - Unbound Medicine ER -