PUBLICATION
Evolution of the vertebrate cytosolic malate dehydrogenase gene family: duplication and divergence in actinopterygian fish
- Authors
- Merrit, T.J.S. and Quattro, M.
- ID
- ZDB-PUB-040129-1
- Date
- 2003
- Source
- Journal of molecular evolution 56(3): 265-276 (Journal)
- Registered Authors
- Keywords
- Malate dehydrogenase, Gene duplication, Neural expression, Positive selection, Ancestral reconstruction, Teleost fish
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Cytosol/enzymology
- Evolution, Molecular*
- Fishes/genetics*
- Gene Duplication*
- Malate Dehydrogenase/genetics*
- Molecular Sequence Data
- Multigene Family*
- Phylogeny
- PubMed
- 12612830 Full text @ J. Mol. Evol.
Citation
Merrit, T.J.S. and Quattro, M. (2003) Evolution of the vertebrate cytosolic malate dehydrogenase gene family: duplication and divergence in actinopterygian fish. Journal of molecular evolution. 56(3):265-276.
Abstract
A general correlation between neural expression and negative charge in isozymes suggests charge represents an adaptation to the neural environment. Interestingly, a notable exception exists in teleost fish. Two cytosolic malate dehydrogenase (MDH) isozymes have different spatial expression patterns in certain fishes: one is expressed in all tissues and the second is expressed primarily in the eye and skeletal muscle. While the neural MDH isozyme is negatively charged, the difference in charge between the two isozymes is not as pronounced as that observed in other gene families (e.g., triosephosphate isomerase and lactate dehydrogenase). Most tetrapods express a single cytosolic MDH isozyme, and it has been demonstrated recently that the pair of isozymes found in teleosts results from a gene duplication sometime after the separation of teleosts and tetrapods, although the exact timing of this duplication has not been inferred. Phylogenetic analyses suggest that the duplication of teleost isozymes occurred during the radiation of actinopterygian fish, consistent with the timing of duplication at other loci. Using inferred amino acid sequences, we examine the pattern of change following the duplication and across the rest of the MDH gene tree. Comparison between the MDH gene family and another gene family that shows a larger charge differential among members (triosephosphate isomerase) indicates that the smaller charge difference between MDH isozymes is best explained by greater constraint on amino acid change directly following the duplication, not greater constraint across the entire gene tree. This difference in constraint might result from the wider pattern of expression of the "neural" MDH isozyme.
Errata / Notes
Erratum in: J Mol Evol. 2003 Jun;56(6):779.Thomas J.S. Merritt’s name was mispelled on the title page of this article as it appeared in the printed issue. We sincerely apologize for the error, and present his name correctly above.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping