Plant Molecular Biology

, Volume 14, Issue 6, pp 1019–1030

Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA clones and primary structure of the higher-plant precursor protein

  • Christine Gietl
  • Michael Lehnerer
  • Ole Olsen

DOI: 10.1007/BF00019398

Cite this article as:
Gietl, C., Lehnerer, M. & Olsen, O. Plant Mol Biol (1990) 14: 1019. doi:10.1007/BF00019398


The isolation and sequence of a cDNA clone encoding the complete mitochondrial malate dehydrogenase (mMDH) of watermelon cotyledons is presented. Taking advantage of the polymerase chain reaction technology partial cDNA clones from the central part, the 3′ part and the 5′ part of the mRNA were obtained with oligonucleotides based on directly determined amino acid sequences. Subsequently, two complete cDNA clones for mMDH were synthesized with a sense primer corresponding to the nucleotide sequence of the amino terminal end of pre-mMDH and two antisense primers corresponding to the major alternative adenylation sites found in the mRNA.

The amino acid residues for substrate and cofactor binding identified by X-ray crystallography for pig heart cytoplasmic MDH are conserved in the 320 amino acid long mature higher-plant mMDH. A presequence of 27 amino acids is present at the amino terminal end of the precursor protein.

Key words

isoenzymes cotyledons Citrullus vulgaris polymerase chain reaction 

Copyright information

© Kluwer Academic Publishers 1990

Authors and Affiliations

  • Christine Gietl
    • 1
  • Michael Lehnerer
    • 1
  • Ole Olsen
    • 2
  1. 1.Lehrstuhl für BotanikTechnische Universität MünchenMünchen 2FRG
  2. 2.Department of PhysiologyCarlsberg LaboratoryValbyDenmark

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