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PMID: 2102869 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Plant molecular biology ·Vol. 14 ·No. 6 ·1990-06-00 ·Pages 1019-30

Gietl C, Lehnerer M, Olsen O

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cloning, Molecular DNA/genetics Fruit/enzymology,genetics Malate Dehydrogenase/genetics Mitochondria/enzymology Molecular Sequence Data Plants/enzymology,genetics Protein Precursors/genetics Restriction Mapping Sequence Homology, Nucleic Acid Species Specificity
Chemicals
Protein Precursors DNA Malate Dehydrogenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Gietl C
Lehrstuhl für Botanik, Technische Universität München, FRG.
Lehnerer M
Olsen O
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34 references, click to expand
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Article Info
Journal
Plant molecular biology
Abbr.
Plant Mol Biol
ISSN
0167-4412
DOI
10.1007/BF00019398
Published
1990-06-00
Pages
1019-30
Language
English
Region
Netherlands
NLM ID
9106343
Subset
IM
Databases
GENBANK
M33148, X17362
External Links
PubMed source DOI: 10.1007/BF00019398 View journal details
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