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Molecular and functional characterization of the plastid‐localized Phosphoenolpyruvate enolase (ENO1) from Arabidopsis thaliana
Author(s) -
Prabhakar Veena,
Löttgert Tanja,
Gigolashvili Tamara,
Bell Kirsten,
Flügge Ulf-Ingo,
Häusler Rainer E.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.02.017
Subject(s) - plastid , arabidopsis thaliana , enolase , biology , trichome , phosphoenolpyruvate carboxykinase , shikimate pathway , biochemistry , arabidopsis , mutant , botany , gene , biosynthesis , chloroplast , immunology , immunohistochemistry
The Arabidopsis thaliana gene At1g74030 codes for a putative plastid phosphoenolpyruvate (PEP) enolase (ENO1). The recombinant ENO1 protein exhibited enolase activity and its kinetic properties were determined. ENO1 is localized to plastids and expressed in most heterotrophic tissues including trichomes and non‐root‐hair cells, but not in the mesophyll of leaves. Two T‐DNA insertion eno1 mutants exhibited distorted trichomes and reduced numbers of root hairs as the only visible phenotype. The essential role of ENO1 in PEP provision for anabolic processes within plastids, such as the shikimate pathway, is discussed with respect to plastid transporters, such as the PEP/phosphate translocator.