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D- and L-lactate dehydrogenases during invertebrate evolution.

Cristescu ME, Innes DJ, Stillman JH, Crease TJ - BMC Evol. Biol. (2008)

Bottom Line: The genes encoding L-LDH have been used as a model for gene duplication due to the multiple paralogs found in eubacteria, archaebacteria, and eukaryotes.While most invertebrates preferentially oxidize L-lactic acid, several species of mollusks, a few arthropods and polychaetes were found to have exclusively D-LDH enzymatic activity.Several amino acid sequences with strong similarity to putative mammalian D-LDH and to yeast DLD1 with D-LDH activity were found in both vertebrates and invertebrates.

View Article: PubMed Central - HTML - PubMed

Affiliation: University of Windsor, Great Lakes Institute for Environmental Research, 401 Sunset Avenue, Windsor, Ontario, N9B 3P4, Canada. mcris@uwindsor.ca

ABSTRACT

Background: The L-lactate and D-lactate dehydrogenases, which are involved in the reduction of pyruvate to L(-)-lactate and D(+)-lactate, belong to evolutionarily unrelated enzyme families. The genes encoding L-LDH have been used as a model for gene duplication due to the multiple paralogs found in eubacteria, archaebacteria, and eukaryotes. Phylogenetic studies have suggested that several gene duplication events led to the main isozymes of this gene family in chordates, but little is known about the evolution of L-Ldh in invertebrates. While most invertebrates preferentially oxidize L-lactic acid, several species of mollusks, a few arthropods and polychaetes were found to have exclusively D-LDH enzymatic activity. Therefore, it has been suggested that L-LDH and D-LDH are mutually exclusive. However, recent characterization of putative mammalian D-LDH with significant similarity to yeast proteins showing D-LDH activity suggests that at least mammals have the two naturally occurring forms of LDH specific to L- and D-lactate. This study describes the phylogenetic relationships of invertebrate L-LDH and D-LDH with special emphasis on crustaceans, and discusses gene duplication events during the evolution of L-Ldh.

Results: Our phylogenetic analyses of L-LDH in vertebrates are consistent with the general view that the main isozymes (LDH-A, LDH-B and LDH-C) evolved through a series of gene duplications after the vertebrates diverged from tunicates. We report several gene duplication events in the crustacean, Daphnia pulex, and the leech, Helobdella robusta. Several amino acid sequences with strong similarity to putative mammalian D-LDH and to yeast DLD1 with D-LDH activity were found in both vertebrates and invertebrates.

Conclusion: The presence of both L-Ldh and D-Ldh genes in several chordates and invertebrates suggests that the two enzymatic forms are not necessarily mutually exclusive. Although, the evolution of L-Ldh has been punctuated by multiple events of gene duplication in both vertebrates and invertebrates, a shared evolutionary history of this gene in the two groups is apparent. Moreover, the high degree of sequence similarity among D-LDH amino acid sequences suggests that they share a common evolutionary history.

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Neighbor-joining tree based on 49 L-Lactate dehydrogenase amino acid sequences from 31 taxa. Numbers at nodes indicate the Neighbour-joining and Maximum Parsimony percentage bootstrap support with 2,000 and 100 replicates, respectively. Nodes supported only by the Neighbor-Joining analysis show a single bootstrap value. The scale bar indicates levels of amino acid sequence divergence. The tree was rooted using the plant LDH sequences.
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Figure 1: Neighbor-joining tree based on 49 L-Lactate dehydrogenase amino acid sequences from 31 taxa. Numbers at nodes indicate the Neighbour-joining and Maximum Parsimony percentage bootstrap support with 2,000 and 100 replicates, respectively. Nodes supported only by the Neighbor-Joining analysis show a single bootstrap value. The scale bar indicates levels of amino acid sequence divergence. The tree was rooted using the plant LDH sequences.

Mentions: Phylogenetic trees generated by MP and Neighbor-joining (NJ, Figure 1) and Bayesian Inference (BI, Figure 2) all support a deuterostome cluster. The only exception is the echinoderm, Strongylocentrotus purpuratus, which groups with nematodes, although bootstrap support for this phylogenetic relationship is extremely low (Figure 1). The vertebrate sequences form a well-supported cluster with the LDH-A and LDH-B isozymes separating into distinct groups. Even so, there are examples of species whose A, B and C isozymes cluster with one another (e.g. Xenopus laevis).


D- and L-lactate dehydrogenases during invertebrate evolution.

Cristescu ME, Innes DJ, Stillman JH, Crease TJ - BMC Evol. Biol. (2008)

Neighbor-joining tree based on 49 L-Lactate dehydrogenase amino acid sequences from 31 taxa. Numbers at nodes indicate the Neighbour-joining and Maximum Parsimony percentage bootstrap support with 2,000 and 100 replicates, respectively. Nodes supported only by the Neighbor-Joining analysis show a single bootstrap value. The scale bar indicates levels of amino acid sequence divergence. The tree was rooted using the plant LDH sequences.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2570690&req=5

Figure 1: Neighbor-joining tree based on 49 L-Lactate dehydrogenase amino acid sequences from 31 taxa. Numbers at nodes indicate the Neighbour-joining and Maximum Parsimony percentage bootstrap support with 2,000 and 100 replicates, respectively. Nodes supported only by the Neighbor-Joining analysis show a single bootstrap value. The scale bar indicates levels of amino acid sequence divergence. The tree was rooted using the plant LDH sequences.
Mentions: Phylogenetic trees generated by MP and Neighbor-joining (NJ, Figure 1) and Bayesian Inference (BI, Figure 2) all support a deuterostome cluster. The only exception is the echinoderm, Strongylocentrotus purpuratus, which groups with nematodes, although bootstrap support for this phylogenetic relationship is extremely low (Figure 1). The vertebrate sequences form a well-supported cluster with the LDH-A and LDH-B isozymes separating into distinct groups. Even so, there are examples of species whose A, B and C isozymes cluster with one another (e.g. Xenopus laevis).

Bottom Line: The genes encoding L-LDH have been used as a model for gene duplication due to the multiple paralogs found in eubacteria, archaebacteria, and eukaryotes.While most invertebrates preferentially oxidize L-lactic acid, several species of mollusks, a few arthropods and polychaetes were found to have exclusively D-LDH enzymatic activity.Several amino acid sequences with strong similarity to putative mammalian D-LDH and to yeast DLD1 with D-LDH activity were found in both vertebrates and invertebrates.

View Article: PubMed Central - HTML - PubMed

Affiliation: University of Windsor, Great Lakes Institute for Environmental Research, 401 Sunset Avenue, Windsor, Ontario, N9B 3P4, Canada. mcris@uwindsor.ca

ABSTRACT

Background: The L-lactate and D-lactate dehydrogenases, which are involved in the reduction of pyruvate to L(-)-lactate and D(+)-lactate, belong to evolutionarily unrelated enzyme families. The genes encoding L-LDH have been used as a model for gene duplication due to the multiple paralogs found in eubacteria, archaebacteria, and eukaryotes. Phylogenetic studies have suggested that several gene duplication events led to the main isozymes of this gene family in chordates, but little is known about the evolution of L-Ldh in invertebrates. While most invertebrates preferentially oxidize L-lactic acid, several species of mollusks, a few arthropods and polychaetes were found to have exclusively D-LDH enzymatic activity. Therefore, it has been suggested that L-LDH and D-LDH are mutually exclusive. However, recent characterization of putative mammalian D-LDH with significant similarity to yeast proteins showing D-LDH activity suggests that at least mammals have the two naturally occurring forms of LDH specific to L- and D-lactate. This study describes the phylogenetic relationships of invertebrate L-LDH and D-LDH with special emphasis on crustaceans, and discusses gene duplication events during the evolution of L-Ldh.

Results: Our phylogenetic analyses of L-LDH in vertebrates are consistent with the general view that the main isozymes (LDH-A, LDH-B and LDH-C) evolved through a series of gene duplications after the vertebrates diverged from tunicates. We report several gene duplication events in the crustacean, Daphnia pulex, and the leech, Helobdella robusta. Several amino acid sequences with strong similarity to putative mammalian D-LDH and to yeast DLD1 with D-LDH activity were found in both vertebrates and invertebrates.

Conclusion: The presence of both L-Ldh and D-Ldh genes in several chordates and invertebrates suggests that the two enzymatic forms are not necessarily mutually exclusive. Although, the evolution of L-Ldh has been punctuated by multiple events of gene duplication in both vertebrates and invertebrates, a shared evolutionary history of this gene in the two groups is apparent. Moreover, the high degree of sequence similarity among D-LDH amino acid sequences suggests that they share a common evolutionary history.

Show MeSH
Related in: MedlinePlus