Cloning and characterization of an Arabidopsis thaliana cDNA clone encoding an organellar isoform of serine acetyltransferase.
We have cloned an Arabidopsis thaliana cDNA encoding serine acetyltransferase (EC 2.3.1.30) by functional complementation of the Escherichia coli cysE mutant JM15. The cDNA clone Sat-1 conferred serine acetyltransferase activity (with apparent Km for the two substrates acetyl CoA and L-serine of 0.043 and 3.47 mmol/dm3 respectively) on the cysE mutant. The 1515 bp full-length cDNA encodes a deduced protein of 391 amino acids which includes a putative chloroplastic targeting presequence. Northern analysis revealed a single message of 1.5 kb, while Southern hybridisation suggests a small multigene family of related sequences.
Roberts
M A
MA
Plant Sciences Laboratory, Research Division of Environmental and Evolutionary Biology, School of Biological and Medical Sciences, University of St. Andrews, Fife, UK.
Wray
J L
JL
D000123:Acetyltransferases / Q000235:genetics*; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D015388:Organelles / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D051050:Serine O-Acetyltransferase
D018076:DNA, Complementary; D000123:Acetyltransferases; D051050:Serine O-Acetyltransferase