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Cloning and primary structure of putative cytosolic and mitochondrial malate dehydrogenase from the mollusc Nucella lapillus (L.)
Kirby, R.R. (2000). Cloning and primary structure of putative cytosolic and mitochondrial malate dehydrogenase from the mollusc Nucella lapillus (L.). Gene 245(1): 81-88. hdl.handle.net/10.1016/S0378-1119(00)00036-6
In: Gene. ELSEVIER SCIENCE BV: Tokyo; Oxford; New York; Lausanne; Shannon; Amsterdam. ISSN 0378-1119, more
Peer reviewed article  

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Keywords
    Evolution; Invertebrates; Marine
Author keywords
    Degenerate; MDH

Author  Top 
  • Kirby, R.R.

Abstract
    The evolutionary history of the malate dehydrogenase (MDH) gene family [NAD-dependent MDH; EC 1.1.1.37 and NAD(P)-dependent MDH; EC 1.1.1.82] has received much attention. MDHs have also featured extensively as electrophoretic markers in population genetics and evolutionary ecology, and in many cases, intraspecific variation in MDH has been correlated with environmental variables. However, while the amino acid residues essential for MDH function are known, no studies have examined intraspecific nucleotide variation despite evidence indicating that natural selection may be operating on this locus. This study presents two sets of degenerate oligonucleotide PCR primers to facilitate the cloning of cytosolic MDH (cMDH) and mitochondrial MDH (mMDH) from a broad range of animals (cMDH) and animals and plants (mMDH). These primers were used to obtain putative cMDH and mMDH cDNAs from the mollusc Nucella lapillus. The N. lapilluscMDH cDNA was found to encode a putative cMDH protein of 334 aa and 36 kDa, while the mMDH cDNA encoded a putative mature mMDH protein of 315 aa and 33 kDa. The putative amino acid sequences of the two compartmentalised N. lapillus MDHs are presented and compared to other known MDH sequences.

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