Evolution of the myoglobin gene in Antarctic Icefishes (Channichthyidae)

Borley, Kimberly A.; Sidell, Bruce D.

doi:10.1007/s00300-010-0921-x

Cited by 9 publications

(8 citation statements)

References 21 publications

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“…The lack of myoglobin expression in skeletal muscle is displayed by both white- and red-blooded notothenioids (Sidell et al 1997; Moylan and Sidell 2000). All icefish completely lack hemoglobin (Ruud 1954), and six species do not express myoglobin in cardiac myocytes (Borley and Sidell 2010). Thus, oxygen supply and ATP generation are extremely challenging in white-blooded icefish.…”

Section: Discussionmentioning

confidence: 99%

“…Icefish do not express myoglobin in skeletal muscle, and six members of the family have lost the ability to produce the protein in cardiac myocytes either, exacerbating their hemoglobinless condition (Borley and Sidell 2010). Adequate oxygen delivery to tissues, even in the absence of respiratory pigments, is ensured in icefish thanks to the evolution of peculiar phenotypic traits such as hypertrophic heart, high cardiac output, increased blood volume, enlarged vessels lumina, low blood viscosity and pressure, well-perfused gills, improved skin and fin vascularization, cutaneous uptake of oxygen, and reduced metabolic rate (Kock 2005).…”

Section: Introductionmentioning

confidence: 99%

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Genome Evolution in the Cold: Antarctic Icefish Muscle Transcriptome Reveals Selective Duplications Increasing Mitochondrial Function

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Agostini

Marino

et al. 2012

Genome Biology and Evolution

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Antarctic notothenioids radiated over millions of years in subzero waters, evolving peculiar features, such as antifreeze glycoproteins and absence of heat shock response. Icefish, family Channichthyidae, also lack oxygen-binding proteins and display extreme modifications, including high mitochondrial densities in aerobic tissues. A genomic expansion accompanying the evolution of these fish was reported, but paucity of genomic information limits the understanding of notothenioid cold adaptation. We reconstructed and annotated the first skeletal muscle transcriptome of the icefish Chionodraco hamatus providing a new resource for icefish genomics (http://compgen.bio.unipd.it/chamatusbase/, last accessed December 12, 2012). We exploited deep sequencing of this energy-dependent tissue to test the hypothesis of selective duplication of genes involved in mitochondrial function. We developed a bioinformatic approach to univocally assign C. hamatus transcripts to orthology groups extracted from phylogenetic trees of five model species. Chionodraco hamatus duplicates were recorded for each orthology group allowing the identification of duplicated genes specific to the icefish lineage. Significantly more duplicates were found in the icefish when transcriptome data were compared with whole-genome data of model species. Indeed, duplicated genes were significantly enriched in proteins with mitochondrial localization, involved in mitochondrial function and biogenesis. In cold conditions and without oxygen-carrying proteins, energy production is challenging. The combination of high mitochondrial densities and the maintenance of duplicated genes involved in mitochondrial biogenesis and aerobic respiration might confer a selective advantage by improving oxygen diffusion and energy supply to aerobic tissues. Our results provide new insights into the genomic basis of icefish cold adaptation.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Genome Evolution in the Cold: Antarctic Icefish Muscle Transcriptome Reveals Selective Duplications Increasing Mitochondrial Function

Coppe

Agostini

Marino

et al. 2012

Genome Biology and Evolution

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“…One possibility is that the identified AA substitutions do not reflect or accurately predict rhodopsin wavelength absorption changes. The wavelength absorption changes caused by STS substitutions have been well tested in previous studies (Table 3; Bischoff et al, 2012;Borley & Sidell, 2011;Fasick & Robinson, 1998;Hill et al, 2019;Hunt et al, 2001). However, the effects of AA changes at other sites (e.g.…”

Section: Relationship Between Habitat Diversification and Rhodopsin E...mentioning

confidence: 89%

Molecular evolution and convergence of the rhodopsin gene in Gymnogobius, a goby group having diverged into coastal to freshwater habitats

Ito

Harada

Tabata

et al. 2021

J of Evolutionary Biology

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The visual system in animals serves a key role in adaptation to a new environment, sexual selection and speciation due to its deep links to fitness through food search, predation avoidance and mate recognition. Therefore, evolutionary patterns of change in the visual system is a crucial topic for understanding evolutionary responses to natural and sexual selection (Seehausen et al., 2008). Opsin genes are often focused on as vision-related genes in studies of adaptive evolution (Lin et al., 2017). Structural changes in the proteins encoded by opsin genes are directly related to changes in visual function (Bowmaker, 2008); hence, opsin genes enable examination of the relationship between amino acid (AA) substitutions and visual adaptation. Furthermore, phylogenetic patterns of structural and functional changes in opsin genes can provide deep insights into evolutionary relationships between ecological changes and the visual system-especially in groups that have undergone adaptive radiation. Such phylogenetic patterns can be influenced by new

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“…In addition to the loss of Hb, many species within the Channichthyid family lack Mb, an intracellular oxygen-binding protein found in muscle. In total, six out of 16 icefish species lack Mb expression in their heart ventricles, a loss that has occurred through four different mutational events Grove et al, 2004;Borley and Sidell, 2011). Lack of Mb expression has important functional effects (Acierno, et al, 1997), but overall significance in the long term may be less than that of Hb loss because the Mb deficit has evolved repeatedly in teleost fishes, whereas it appears that Hb deletion has been restricted to notothenioids alone (Macqueen et al, 2014).…”

Section: Loss Of Major Hemoproteinsmentioning

confidence: 99%

Antarctic notothenioid fish: what are the future consequences of ‘losses’ and ‘gains’ acquired during long-term evolution at cold and stable temperatures?

Beers

Jayasundara

2015

Journal of Experimental Biology

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Antarctic notothenioids dominate the fish fauna of the Southern Ocean. Evolution for millions of years at cold and stable temperatures has led to the acquisition of numerous biochemical traits that allow these fishes to thrive in sub-zero waters. The gain of antifreeze glycoproteins has afforded notothenioids the ability to avert freezing and survive at temperatures often hovering near the freezing point of seawater. Additionally, possession of cold-adapted proteins and membranes permits them to sustain appropriate metabolic rates at exceptionally low body temperatures. The notothenioid genome is also distinguished by the disappearance of traits in some species, losses that might prove costly in a warmer environment. Perhaps the best-illustrated example is the lack of expression of hemoglobin in white-blooded icefishes from the family Channichthyidae. Loss of key elements of the cellular stress response, notably the heat shock response, has also been observed. Along with their attainment of cold tolerance, notothenioids have developed an extreme stenothermy and many species perish at temperatures only a few degrees above their habitat temperatures. Thus, in light of today's rapidly changing climate, it is critical to evaluate how these extreme stenotherms will respond to rising ocean temperatures. It is conceivable that the remarkable cold specialization of notothenioids may ultimately leave them vulnerable to future thermal increases and threaten their fitness and survival. Within this context, our review provides a current summary of the biochemical losses and gains that are known for notothenioids and examines these cold-adapted traits with a focus on processes underlying thermal tolerance and acclimation capacity.

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Evolution of the myoglobin gene in Antarctic Icefishes (Channichthyidae)

Cited by 9 publications

References 21 publications

Genome Evolution in the Cold: Antarctic Icefish Muscle Transcriptome Reveals Selective Duplications Increasing Mitochondrial Function

Genome Evolution in the Cold: Antarctic Icefish Muscle Transcriptome Reveals Selective Duplications Increasing Mitochondrial Function

Molecular evolution and convergence of the rhodopsin gene in Gymnogobius, a goby group having diverged into coastal to freshwater habitats

Antarctic notothenioid fish: what are the future consequences of ‘losses’ and ‘gains’ acquired during long-term evolution at cold and stable temperatures?

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