Higher-plant cofactor-independent phosphoglyceromutase: purification, molecular characterization and expression.

Cofactor-independent phosphoglyceromutase (PGM) was purified to homogeneity from developing castor seed endosperm. Immunological characterization using monospecific antisera raised against this protein indicates that the enzyme is located in the cytosol and that there is no immunologically related polypeptide in the leucoplast from this tissue. Isolation and sequence determination of full-length cDNA clones for castor and tobacco PGM demonstrate that the protein is highly conserved in these plants and is closely related to the maize enzyme. A comparison of the amino acid sequence of peptides derived from Neurospora crassa PGM with the cofactor-independent enzyme from higher plants demonstrated that they are related and may have diverged from a common ancestral gene. The previously proposed relationship between higher-plant PGM and alkaline phosphatases is not supported by sequence analysis of the castor and tobacco enzymes. Expression of the single castor cytosolic PGM gene correlates well with other cytosolic glycolytic genes in developing and germinating castor seeds, and with the appearance of enzyme activity and PGM polypeptides in these tissues.