2,3-Bisphosphoglycerate-independent phosphoglycerate mutase is conserved among different phylogenic kingdoms.
We have previously demonstrated that maize (Zea mays) 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (PGAM-i) is not related to 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. With the aid of specific anti-maize PGAM-i antibodies, we demonstrate here the presence of a closely related PGAM-i in other plants. We also describe the isolation and sequencing of a cDNA-encoding almond (Prunus amygdalus) PGAM-i that further demonstrates this relationship among plant PGAM-i. A search of the major databases for related sequences allowed us to identify some novel PGAM-i from different sources: plants (Arabidopsis thaliana, Oryza sativa and Antithamniom sp.), monera (Escherichia coli, Bacillus subtilis and Bacillus megaterium) and animals (Caenorhabditis elegans). All of these amino acid sequences share a high degree of homology with plant PGAM-i. These observations suggest that the PGAM-i from several biological kingdoms constitute a family of protein different from other proteins with related enzymatic function and arose from a common ancestral gene that has diverged throughout its evolution.
Graña
X
X
Unitat de Bioquimica, Facultat de Medicina, Universitat de Barcelona, Spain.
Pérez de la Ossa
P
P
Broceño
C
C
Stöcker
M
M
Garriga
J
J
Puigdomènech
P
P
Climent
F
F
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria; D005075:Biological Evolution; D017124:Conserved Sequence; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010736:Phosphoglycerate Mutase / Q000235:genetics*; D010944:Plants; D016415:Sequence Alignment; D017421:Sequence Analysis
D018076:DNA, Complementary; D010736:Phosphoglycerate Mutase