Title: TREHALOSE-6-PHOSPHATE SYNTHASE 1 is not the only active TPS in Arabidopsis thaliana
Authors: Delorge, Ines ×
Figueroa, Carlos M
Feil, Regina
Lunn, John E
Van Dijck, Patrick #
Issue Date: 1-Mar-2015
Publisher: Published by Portland Press on behalf of the Biochemical Society
Series Title: Biochemical Journal vol:466 issue:2 pages:283-290
Abstract: Trehalose metabolism is essential for normal growth and development in higher plants. It is synthesized in a two-step pathway catalyzed by trehalose-6-phosphate (Tre6P) synthase (TPS) and trehalose phosphatase. Arabidopsis thaliana has 11 TPS or TPS-like proteins, which belong to two distinct clades: class I (AtTPS1-AtTPS4) and class II (AtTPS5-AtTPS11). Only AtTPS1 has previously been shown to have TPS activity. Null A. thaliana tps1 mutants fail to complete embryogenesis and rescued lines have stunted growth and delayed flowering, indicating that AtTPS1 is important throughout the life cycle. Here we show that expression of AtTPS2 or AtTPS4 enables the yeast tps1∆ tps2∆ mutant to grow on glucose and accumulate Tre6P and trehalose. Class II TPS genes did not complement the yeast mutant. Thus, A. thaliana has at least three catalytically active TPS isoforms, suggesting that loss of Tre6P production might not be the only reason for the growth defects of A. thaliana tps1 mutants.
ISSN: 0264-6021
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Microbiology and Biotechnology Section - miscellaneous
× corresponding author
# (joint) last author

Files in This Item:
File Description Status SizeFormat
bj2014-1322a.pdf Published 1005KbAdobe PDFView/Open Request a copy

These files are only available to some KU Leuven Association staff members


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science