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Nucleic Acids Research, 1986, Vol. 14, No. 4 1615-1628
© 1986

Articles

Cloning and sequence analysis of cDNA encoding active phosphoenolpyruvate carboxylase of the C4-pathway from maize

Katsura Izui, Sumio Ishijima, Yasunori Yamaguchi*,, Fumiaki Katagiri, Takuya Murata, Katsuya Shigesada1, Tatsuo Sugiyama2 and Hirohiko Katsuki3

Department of Chemistry, Faculty of Science, Kyoto University Kyoto 606 1Department of Biochemistry, Institute for Virus Research, Kyoto University Kyoto 606 2Department of Agricultural Chemistry, Faculty of Agriculture, Nagoya University Nagoya 464 3College of Liberal Arts, Kinki University Higashiosaka, Osaka 577, Japan

Received December 25, 1985. Accepted January 22, 1986.

A recombinant clone, pM52, containing cDNA for maize phosphoenolpyruvate carboxylase (PEPCase, EC 4. 1.1.31) was isolated from a maize leaf cDNA library constructed using an expression vector in Escherichia coli. The screening of the clone was conveniently performed through its ability to complement the phenotype (glutamate requirement) of PEPCase-negative mutant of E. coli. The enzyme encoded by this clone was identical with the major PEPCase in maize, a key enzyme in the C4-pathway, as judged from its allosteric properties and immunological reactivity. The cloned cDNA (3093 nucleotides in length) contained an open reading frame of 2805 nucleotides, the 3'-untranslated region of 222 nucleotides and the poly(dA) tract of 64 nucleotides. The deduced amino acid sequence (935 residues) of the enzyme showed higher homology with that of an enterobacterium, E. coli (43%) than that of a cyanobacterium (blue-green alga), Anacystis nidulans (33%).

*Present address: Department of Zoology, Faculty of Science, Kyoto University, Kyoto 606, Japan.


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