Sequence comparison of glyceraldehyde-3-phosphate dehydrogenases from the three urkingdoms: evolutionary implication.
The primary structure of the glyceraldehyde-3-phosphate dehydrogenase from the archaebacteria shows striking deviation from the known sequences of eubacterial and eukaryotic sequences, despite unequivocal homologies in functionally important regions. Thus, the structural similarity between the eubacterial and eukaryotic enzymes is significantly higher than that between the archaebacterial enzymes and the eubacterial and eukaryotic enzymes. This preferred similarity of eubacterial and eukaryotic glyceraldehyde-3-phosphate dehydrogenase structures does not correspond to the phylogenetic distances among the three urkingdoms as deduced from comparisons of ribosomal ribonucleic acid sequences. Indications will be presented that the closer relationship of the eubacterial and eukaryotic glyceraldehyde-3-phosphate dehydrogenase resulted from a gene transfer from eubacteria to eukaryotes after the segregation of the three urkingdoms.
Hensel
R
R
Max-Planck-Institut f. Biochemie, Martinsried, Federal Republic of Germany.
Zwickl
P
P
Fabry
S
S
Lang
J
J
Palm
P
P
D000595:Amino Acid Sequence; D000818:Animals; D001105:Archaea / Q000201:enzymology / Q000235:genetics; D005075:Biological Evolution; D005051:Eubacterium / Q000201:enzymology / Q000235:genetics; D005057:Eukaryotic Cells / Q000201:enzymology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000235:genetics*; D008969:Molecular Sequence Data; D013045:Species Specificity; D014162:Transfection
D005987:Glyceraldehyde-3-Phosphate Dehydrogenases