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The evolutionary fate of alternatively spliced homologous exons after gene duplication.

Abascal F, Tress ML, Valencia A - Genome Biol Evol (2015)

Bottom Line: We found examples supporting two extreme evolutionary models for the behaviour of homologous axons after gene duplication.At other extreme, we identified genes in which the homologous exons were always conserved within paralogs, suggesting that the alternative splicing event cannot easily be separated from the function in these genes.That many homologous exons fall in between these two extremes highlights the diversity of biological systems and suggests that the subtle balance between alternative splicing and gene duplication is adjusted to the specific cellular context of each gene.

View Article: PubMed Central - PubMed

Affiliation: Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), Madrid, Spain fabascal@cnio.es mtress@cnio.es.

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The multiple sequence alignment (A) of a pair of MEHEs from different alpha actinins (corresponding to exons 8a and 8b in human ACTN2) reveals the ancient ancestry of this AS event (it first appeared in the ancestor of bilaterians) and how the original pattern has been conserved in multiple gene lineages despite several GD events. Alternatively spliced MEHEs are highlighted by using same colors. Human ACTN4 has two MEHE events, one conserved in ACTN2 (see above) and another that is found in ACTN1, which are spatially close in the 3D dimeric structure of alpha actinin, within the actin-binding regions shown in (B). The structure corresponds to the cryoEM model of chicken ACTN1 (pdb:1SJJ; Liu et al. 2004).
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evv076-F5: The multiple sequence alignment (A) of a pair of MEHEs from different alpha actinins (corresponding to exons 8a and 8b in human ACTN2) reveals the ancient ancestry of this AS event (it first appeared in the ancestor of bilaterians) and how the original pattern has been conserved in multiple gene lineages despite several GD events. Alternatively spliced MEHEs are highlighted by using same colors. Human ACTN4 has two MEHE events, one conserved in ACTN2 (see above) and another that is found in ACTN1, which are spatially close in the 3D dimeric structure of alpha actinin, within the actin-binding regions shown in (B). The structure corresponds to the cryoEM model of chicken ACTN1 (pdb:1SJJ; Liu et al. 2004).

Mentions: The importance of AS is particularly clear in the case of human ACTN2 and ACTN4 genes, which code for alpha-actinin 2 and 4, respectively. Alpha-actinins are important cytoskeletal proteins with multiple roles and many interacting partners. Interestingly, some of these partners also have MEHEs, for example PDLIM3, with MEHEs that affect a region involved in actinin-binding. The actinin family has two pairs of MEHEs that are distant in sequence, but close in the dimeric structure (fig. 5B). In human, ACTN4 has both pairs of MEHEs, ACTN1 and ACTN2 each share a different pair of MEHEs with ACTN4, and ACTN3 has no MEHEs.Fig. 5.—


The evolutionary fate of alternatively spliced homologous exons after gene duplication.

Abascal F, Tress ML, Valencia A - Genome Biol Evol (2015)

The multiple sequence alignment (A) of a pair of MEHEs from different alpha actinins (corresponding to exons 8a and 8b in human ACTN2) reveals the ancient ancestry of this AS event (it first appeared in the ancestor of bilaterians) and how the original pattern has been conserved in multiple gene lineages despite several GD events. Alternatively spliced MEHEs are highlighted by using same colors. Human ACTN4 has two MEHE events, one conserved in ACTN2 (see above) and another that is found in ACTN1, which are spatially close in the 3D dimeric structure of alpha actinin, within the actin-binding regions shown in (B). The structure corresponds to the cryoEM model of chicken ACTN1 (pdb:1SJJ; Liu et al. 2004).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4494069&req=5

evv076-F5: The multiple sequence alignment (A) of a pair of MEHEs from different alpha actinins (corresponding to exons 8a and 8b in human ACTN2) reveals the ancient ancestry of this AS event (it first appeared in the ancestor of bilaterians) and how the original pattern has been conserved in multiple gene lineages despite several GD events. Alternatively spliced MEHEs are highlighted by using same colors. Human ACTN4 has two MEHE events, one conserved in ACTN2 (see above) and another that is found in ACTN1, which are spatially close in the 3D dimeric structure of alpha actinin, within the actin-binding regions shown in (B). The structure corresponds to the cryoEM model of chicken ACTN1 (pdb:1SJJ; Liu et al. 2004).
Mentions: The importance of AS is particularly clear in the case of human ACTN2 and ACTN4 genes, which code for alpha-actinin 2 and 4, respectively. Alpha-actinins are important cytoskeletal proteins with multiple roles and many interacting partners. Interestingly, some of these partners also have MEHEs, for example PDLIM3, with MEHEs that affect a region involved in actinin-binding. The actinin family has two pairs of MEHEs that are distant in sequence, but close in the dimeric structure (fig. 5B). In human, ACTN4 has both pairs of MEHEs, ACTN1 and ACTN2 each share a different pair of MEHEs with ACTN4, and ACTN3 has no MEHEs.Fig. 5.—

Bottom Line: We found examples supporting two extreme evolutionary models for the behaviour of homologous axons after gene duplication.At other extreme, we identified genes in which the homologous exons were always conserved within paralogs, suggesting that the alternative splicing event cannot easily be separated from the function in these genes.That many homologous exons fall in between these two extremes highlights the diversity of biological systems and suggests that the subtle balance between alternative splicing and gene duplication is adjusted to the specific cellular context of each gene.

View Article: PubMed Central - PubMed

Affiliation: Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), Madrid, Spain fabascal@cnio.es mtress@cnio.es.

Show MeSH
Related in: MedlinePlus