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1.
Mol Ecol ; 26(12): 3256-3275, 2017 Jun.
Article in English | MEDLINE | ID: mdl-28316106

ABSTRACT

Active transposable elements (TEs) may result in divergent genomic insertion and abundance patterns among conspecific populations. Upon secondary contact, such divergent genetic backgrounds can theoretically give rise to classical Dobzhansky-Muller incompatibilities (DMI), thus contributing to the evolution of endogenous genetic barriers and eventually causing population divergence. We investigated differential TE abundance among conspecific populations of the nonbiting midge Chironomus riparius and evaluated their potential role in causing endogenous genetic incompatibilities between these populations. We focussed on a Chironomus-specific TE, the minisatellite-like Cla-element, whose activity is associated with speciation in the genus. Using a newly generated and annotated draft genome for a genomic study with five natural C. riparius populations, we found highly population-specific TE insertion patterns with many private insertions. A significant correlation of the pairwise FST estimated from genomewide single-nucleotide polymorphisms (SNPs) and the FST estimated from TEs is consistent with drift as the major force driving TE population differentiation. However, the significantly higher Cla-element FST level due to a high proportion of differentially fixed Cla-element insertions also indicates selection against segregating (i.e. heterozygous) insertions. With reciprocal crossing experiments and fluorescent in situ hybridization of Cla-elements to polytene chromosomes, we documented phenotypic effects on female fertility and chromosomal mispairings. We propose that the inferred negative selection on heterozygous Cla-element insertions may cause endogenous genetic barriers and therefore acts as DMI among C. riparius populations. The intrinsic genomic turnover exerted by TEs may thus have a direct impact on population divergence that is operationally different from drift and local adaptation.


Subject(s)
Chironomidae/genetics , DNA Transposable Elements , Genetics, Population , Genome, Insect , Minisatellite Repeats , Animals , Evolution, Molecular , Female , In Situ Hybridization, Fluorescence , Polymorphism, Single Nucleotide
2.
Theory Biosci ; 126(1): 35-42, 2007 Aug.
Article in English | MEDLINE | ID: mdl-18087755

ABSTRACT

The phylogenetic position of Xenoturbella bocki has been a matter of controversy since its description in 1949. We sequenced a second complete mitochondrial genome of this species and performed phylogenetic analyses based on the amino acid sequences of all 13 mitochondrial protein-coding genes and on its gene order. Our results confirm the deuterostome relationship of Xenoturbella. However, in contrast to a recently published study (Bourlat et al. in Nature 444:85-88, 2006), our data analysis suggests a more basal branching of Xenoturbella within the deuterostomes, rather than a sister-group relationship to the Ambulacraria (Hemichordata and Echinodermata).


Subject(s)
DNA, Mitochondrial/genetics , Invertebrates/genetics , Amino Acid Sequence , Animals , Base Sequence , DNA, Mitochondrial/chemistry , Molecular Sequence Data , Phylogeny , Polymerase Chain Reaction , RNA, Transfer/chemistry , RNA, Transfer/genetics , Sequence Alignment
3.
J Inorg Biochem ; 99(1): 110-9, 2005 Jan.
Article in English | MEDLINE | ID: mdl-15598495

ABSTRACT

Neuroglobin and cytoglobin are two recent additions to the family of heme-containing respiratory proteins of man and other vertebrates. Here, we review the present state of knowledge of the structures, ligand binding kinetics, evolution and expression patterns of these two proteins. These data provide a first glimpse into the possible physiological roles of these globins in the animal's metabolism. Both, neuroglobin and cytoglobin are structurally similar to myoglobin, although they contain distinct cavities that may be instrumental in ligand binding. Kinetic and structural studies show that neuroglobin and cytoglobin belong to the class of hexa-coordinated globins with a biphasic ligand-binding kinetics. Nevertheless, their oxygen affinities resemble that of myoglobin. While neuroglobin is evolutionarily related to the invertebrate nerve-globins, cytoglobin shares a more recent common ancestry with myoglobin. Neuroglobin expression is confined mainly to brain and a few other tissues, with the highest expression observed in the retina. Present evidence points to an important role of neuroglobin in neuronal oxygen homeostasis and hypoxia protection, though other functions are still conceivable. Cytoglobin is predominantly expressed in fibroblasts and related cell types, but also in distinct nerve cell populations. Much less is known about its function, although in fibroblasts it might be involved in collagen synthesis.


Subject(s)
Globins , Nerve Tissue Proteins , Amino Acid Sequence , Animals , Cytoglobin , Gene Expression Regulation , Globins/chemistry , Globins/classification , Globins/genetics , Globins/metabolism , Hemeproteins/chemistry , Hemeproteins/classification , Hemeproteins/genetics , Hemeproteins/metabolism , Humans , Models, Molecular , Molecular Sequence Data , Nerve Tissue Proteins/chemistry , Nerve Tissue Proteins/classification , Nerve Tissue Proteins/genetics , Nerve Tissue Proteins/metabolism , Neuroglobin , Phylogeny , Protein Conformation , Sequence Alignment
4.
Mol Biol Evol ; 19(4): 416-21, 2002 Apr.
Article in English | MEDLINE | ID: mdl-11919282

ABSTRACT

Vertebrates possess multiple respiratory globins that differ in terms of structure, function, and tissue distribution. Three types of globins have been described so far: hemoglobin facilitates the transport of oxygen in the blood, myoglobin serves oxygen transport and storage in the muscle, and neuroglobin has a yet unidentified function in nerve cells. Here we report the identification of a fourth and novel type of globin in mouse, man, and zebrafish. It is expressed in apparently all types of human tissue and therefore has been called cytoglobin (CYGB). Mouse and human CYGBs comprise 190 amino acids; the zebrafish CYGB, 174 amino acids. The human CYGB gene is located on chromosome 17q25. The mammalian genes display a unique exon-intron pattern with an additional exon resulting in a C-terminal extension of the protein, which is absent in the fish CYGB. Phylogenetic analyses suggest that the CYGBs had a common ancestor with vertebrate myoglobins. This indicates that the vertebrate myoglobins are in fact a specialized intracellular globin that evolved in adaptation to the special needs of muscle cells.


Subject(s)
Globins/metabolism , Hemoglobins/genetics , Amino Acid Sequence , Animals , Blotting, Northern , Chromosomes, Human, Pair 17/genetics , Cloning, Molecular , Cytoglobin , DNA Primers/chemistry , Exons , Globins/classification , Globins/genetics , Globins/isolation & purification , Humans , Mice , Molecular Sequence Data , Phylogeny , Polymerase Chain Reaction , Sequence Homology, Amino Acid , Tissue Distribution , Zebrafish
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