Mutagenesis of a plastidial lysophosphatidic acid acyltransferase

A combination of site-directed and random mutagenesis generated sequence va riants of a plastidial lysophosphatidic acid acyltransferase. Alanine subst itutions of residues present within two conserved motifs including the puta tive catalytic histidine resulted in a loss of acyltransferase activity ass essed as complementation competance. Substitutions at five sites within the central core resulted in reduced or loss of activity. Truncation mutants r eveal that sequences in the C-terminal moiety are essential for function.