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The malate synthase gene of cucumber

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Abstract

The complete sequences of a full-length cDNA clone and a genomic clone encoding the Cucumis sativus glyoxysomal enzyme malate synthase, have been determined. The sequences have enabled us to identify putative control regions at the 5′ end of the gene, three introns, and possible alternative polyadenylation sites at the 3′ end. The deduced amino acid sequence predicts a polypeptide of 64961 molecular weight, which has 48% identity with that of Escherichia coli. Comparison of the sequence of malate synthase from cucumber with that from E. coli and with other glyoxysomal and peroxisomal enzymes, shows that a conserved C-terminal tripeptide is a common feature of those enzymes imported into microbodies.

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Author notes

  1. Laura M. Smith

    Present address: Department of Biochemistry, University of Leeds, LS2 9JT, Leeds, England, UK

  2. John W. S. Brown

    Present address: Department of Biological Sciences, The University, DD1 4HN, Dundee, Scotland, UK

Authors and Affiliations

  1. Department of Botany, The Kings Buildings, University of Edinburgh, Mayfield Road, EH9 3JH, Edinburgh, Scotland, UK

    Ian A. Graham, Laura M. Smith, John W. S. Brown, Christopher J. Leaver & Steven M. Smith

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  1. Ian A. Graham
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  2. Laura M. Smith
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  3. John W. S. Brown
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  4. Christopher J. Leaver
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  5. Steven M. Smith
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Graham, I.A., Smith, L.M., Brown, J.W.S. et al. The malate synthase gene of cucumber. Plant Mol Biol 13, 673–684 (1989). https://doi.org/10.1007/BF00016022

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