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

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...

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Bibliographic Details
Published in:Plant molecular biology 1990-06, Vol.14 (6), p.1019-1030
Main Authors: Gietl, C. (Technische Univ. Muenchen (Germany). Lehrstuel fuer Botanik), Lehnerer, M, Olsen, O
Format: Article
Language:English
Subjects:
ACIDE AMINE
ADN
Amino Acid Sequence
AMINO ACIDS
AMINOACIDOS
Animals
ARN MENSAJERO
ARN MESSAGER
Base Sequence
Biological and medical sciences
CITRULLUS LANATUS
Citrullus vulgaris
Cloning, Molecular
COTILEDONES
COTYLEDON
COTYLEDONS
DNA
DNA - genetics
Fruit - enzymology
Fruit - genetics
Fundamental and applied biological sciences. Psychology
Genes. Genome
ISOENZIMAS
ISOENZYME
ISOENZYMES
MALATE DEHYDROGENASE
Malate Dehydrogenase - genetics
MALATE DESHYDROGENASE
MALATO DESHIDROGENASA
MESSENGER RNA
MITOCHONDRIA
Mitochondria - enzymology
MITOCHONDRIE
MITOCONDRIA
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Plants - enzymology
Plants - genetics
POLIMERIZACION
POLYMERISATION
POLYMERIZATION
Protein Precursors - genetics
Restriction Mapping
Sequence Homology, Nucleic Acid
Species Specificity
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Summary: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.
ISSN:0167-4412
1573-5028
DOI:10.1007/bf00019398