Cloning and molecular analyses of the Arabidopsis thaliana plastid pyruvate dehydrogenase subunits.
Herein we report the first molecular description of the pyruvate dehydrogenase component of the higher plant plastid pyruvate dehydrogenase complex. The full-length cDNAs for the E1 alpha (1530 bp) and E1 beta (1441 bp) subunits of the Arabidopsis thaliana plastid pyruvate dehydrogenase contain open reading frames that encode polypeptides of 428 and 406 amino acids, respectively, with calculated molecular weight values of 47,120 and 44,208. The deduced amino acid sequences for Arabidopsis plastid E1 alpha and E1 beta have 61% and 68% identity to the odpA and odpB genes of the red alga Porphyra purpurea, respectively, but only 31% and 32% identity to the plant mitochondrial counterparts. Results of Southern analyses suggest that each subunit is encoded by a single gene. Northern blot analyses indicate expression of mRNAs of the appropriate size in Arabidopsis leaves.
Johnston
M L
ML
Department of Biochemistry, University of Missouri, Columbia 65211, USA.
Luethy
M H
MH
Miernyk
J A
JA
Randall
D D
DD
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology*; D003001:Cloning, Molecular; D017343:Genes, Plant; D008969:Molecular Sequence Data; D010802:Phylogeny; D010940:Plant Proteins / Q000235:genetics; D011768:Pyruvate Dehydrogenase Complex / Q000235:genetics*; D018749:RNA, Plant / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D010940:Plant Proteins; D011768:Pyruvate Dehydrogenase Complex; D018749:RNA, Plant