Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “exon shuffle”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

3 recordsLinked to original sources
PubMed2000

The mouse neurological mutant flailer expresses a novel hybrid gene derived by exon shuffling between Gnb5 and Myo5a.

Exon shuffling is thought to be an important mechanism for evolution of new genes. Here we show that the mouse neurological mutation flailer (flr) expresses a novel gene that combines the promoter and first two exons of guanine nucleotide binding protein beta 5 (Gnb5) with the C-terminal exons of the closely linked Myosin 5A (MyoVA) gene (Myo5a). The flailer protein, which is expressed predominantly in brain, contains the N-terminal 83 amino acids of Gnb5 fused in-frame with the C-terminal 711 amino acids of MyoVA, including the globular tail domain that binds organelles for intracellular transport. Biochemical and genetic studies indicate that the flailer protein competes with wild-type MyoVA in vivo, preventing the localization of smooth endoplasmic reticulum vesicles in the dendritic spines of cerebellar Purkinje cells. The flailer protein thus has a dominant-negative mechanism of action with a recessive mode of inheritance due to the dependence of competitive binding on the ratio between mutant and wild-type proteins. The chromosomal arrangement of Myo5a upstream of Gnb5 is consistent with non-homologous recombination as the mutational mechanism. To our knowledge, flailer is the first example of a mammalian mutation caused by germ line exon shuffling between unrelated genes.

Amino Acid Sequence↗
PubMed2026

From neuropeptides to toxins: illuminating the origins of venom complexity in cone snails.

New genes and gene functions are key drivers of evolutionary innovation. Venomous animals, such as cone snails, provide striking examples of gene innovation, yet the mechanisms by which toxins arise remain poorly understood. Using the Conus textile genome, we uncover how neuropeptide genes were recruited into the venom and neofunctionalized as doppelgänger toxins. We identify over 20 independent recruitment events that evolved dynamically across the Conus lineage. Rather than arising from ohnologs of a whole-genome duplication event ∼200 mya, these toxins evolved through diverse mechanisms, including exon shuffling, alternative splicing, and ectopic recombination, often facilitated by lineage-specific transposable elements. Our findings reveal a dynamic interplay between genome architecture and molecular innovation, offering broad insight into the evolution of complex gene repertoires in venoms and beyond.

Animals↗
PubMed2026

Evolutionary history and recombination in the mitochondrial carrier SLC25 superfamily analyzed by similarities in the exon and transmembrane α-helix sequences.

Mitochondrial carriers (MCs), which constitute a superfamily also called the solute carrier family 25 (SLC25), are characterized by conserved signature motif sequences and a six-transmembrane α-helical transporter domain. They transport a wide variety of substrates ranging from protons, inorganic ions, citric acid cycle intermediates, and amino acids to nucleotides and cofactors. The superfamily members can be divided into subfamilies, each with a distinct substrate specificity. In an attempt to understand how different subfamilies have evolved, we analyzed the protein sequences of the exons (with conserved boundaries) and the six transmembrane α-helices of MCs from highly diverged organisms. The results show that some MC subfamilies have all exons and transmembrane α-helices most similar to a closely related subfamily, which is consistent with a scenario of gene duplication and mutational divergence from a last common ancestor. However, several MC subfamilies appear to be mosaics of exons and transmembrane α-helices most similar to different and distant subfamilies, which in some cases could be explained by recombination between the superfamily genes during evolution. It seems that this latter mechanism could have played a role in the formation of new subfamilies with different substrate specificities by the combination of MC transporter domain segments that had been optimized previously for binding specific portions of the substrates. This study presents novel evolutionary relationships between MC subfamilies and may provide clues for how protein superfamilies have expanded and how to investigate their evolution.

Evolution, Molecular↗