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Updated: May 5, 2026

Transient Expression and Cellular Localization of Recombinant Proteins in Cultured Insect Cells
Published on: April 20, 2017
Plant phosphoglucose isomerase genes lack introns and are expressed in Escherichia coli
R C Tait1, B E Froman, D L Laudencia-Chingcuanco
1Department of Genetics, University of California, 95616, Davis, CA, USA.
Abstract:
Nuclear genes that appear to encode both cytosolic and plastid isozymes of phosphoglucose isomerase (PGI), an essential glycolytic enzyme, have been isolated from three diploid species of the annual wild flower genus Clarkia (Onagraceae). The genes do not contain introns and are expressed to varying degrees in Escherichia coli when cloned in either Charon 35 phage or pUC plasmid vectors. The PGI proteins synthesized in E. coli form dimers, are catalytically active, and their electrophoretic mobilities are similar to those of appropriate Clarkia PGIs. The nucleotide sequence of a gene encoding a plastid isozyme of C. unguiculata is described.
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