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Mutagenesis of a plastidial lysophosphatidic acid acyltransferase
S Maisonneuve1, J J Bessoule, R Lessire
1Laboratoire de Génome et Développement des Plantes, CNRS UMR 5096, Université de Perpignan, 52 Avenue de Villeneuve, 66860 Perpignan, France.
Biochemical Society Transactions
|February 15, 2001
Abstract:
A combination of site-directed and random mutagenesis generated sequence variants of a plastidial lysophosphatidic acid acyltransferase. Alanine substitutions of residues present within two conserved motifs including the putative catalytic histidine resulted in a loss of acyltransferase activity assessed as complementation competence. Substitutions at five sites within the central core resulted in reduced or loss of activity. Truncation mutants reveal that sequences in the C-terminal moiety are essential for function.