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Molecular and Biochemical Characterization of Cytosolic Phosphoglucomutase in Maize1
Expression during Development and in Response to Oxygen Deprivation

Sivalinganna Manjunath, Chien-Hsing Kenneth Lee, Patrick Van Winkle, and Julia Bailey-Serres*

Department of Botany and Plant Sciences, University of California, Riverside, California 92521-0124

Phosphoglucomutase (PGM) catalyzes the interconversion of glucose (Glc)-1- and Glc-6-phosphate in the synthesis and consumption of sucrose. We isolated two maize (Zea mays L.) cDNAs that encode PGM with 98.5% identity in their deduced amino acid sequence. Southern-blot analysis with genomic DNA from lines with different Pgm1 and Pgm2 genotypes suggested that the cDNAs encode the two known cytosolic PGM isozymes, PGM1 and PGM2. The cytosolic PGMs of maize are distinct from a plastidic PGM of spinach (Spinacia oleracea). The deduced amino acid sequences of the cytosolic PGMs contain the conserved phosphate-transfer catalytic center and the metal-ion-binding site of known prokaryotic and eukaryotic PGMs. PGM mRNA was detectable by RNA-blot analysis in all tissues and organs examined except silk. A reduction in PGM mRNA accumulation was detected in roots deprived of O2 for 24 h, along with reduced synthesis of a PGM identified as a 67-kD phosphoprotein on two-dimensional gels. Therefore, PGM is not one of the so-called "anaerobic polypeptides." Nevertheless, the specific activity of PGM was not significantly affected in roots deprived of O2 for 24 h. We propose that PGM is a stable protein and that existing levels are sufficient to maintain the flux of Glc-1-phosphate into glycolysis under O2 deprivation.

1   This project was funded by the U.S. Department of Agriculture/National Research Initiative Competitive Grants Program (nos. 92-02016 and 95-00866) and by a University of California-Riverside Academic Senate Research Award.
*   Corresponding author; e-mail serres{at}mail.ucr.edu; fax 1-909-787-3738.

Plant Physiol. (1998) 117: 997-1006
Copyright Clearance Center:   0032-0889/98/117/0997/10
© 1998 American Society of Plant Physiologists




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