Adaptations to environmental change: Globin superfamily evolution in Antarctic fishes

Daane, Jacob M.; Giordano, Daniela; Coppola, Daniela; Prisco, Guido di; Detrich, H. William; Verde, Cinzia

doi:10.1016/j.margen.2019.100724

Cited by 11 publications

(7 citation statements)

References 172 publications

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“…Another example of globin family members substituting for another and presumably assuming the latter's function is illustrated by the elephant shark with expression of α-globin in its nervous tissue whereas its genome appears to be devoid of Ngb [ 99 ]. In sharp contrast to the multiple Mb isoform harbouring genomes, certain Antarctic icefish species ( Channichthyidae family) have completely lost the expression of Mb (and for some also Hb), whose absence is greatly compensated by an adapted cardiovascular system to ensure proper oxygen delivery to the tissues [ [100] , [101] , [102] ]. Notably, also frogs, stickleback fish and the marsupial opossum lack a Mb gene [ 83 , 103 ].…”

Section: Vertebrate Globinsmentioning

confidence: 99%

Lessons from the post-genomic era: Globin diversity beyond oxygen binding and transport

et al. 2020

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Vertebrate hemoglobin (Hb) and myoglobin (Mb) were among the first proteins whose structures and sequences were determined over 50 years ago. In the subsequent pregenomic period, numerous related proteins came to light in plants, invertebrates and bacteria, that shared the myoglobin fold, a signature sequence motif characteristic of a 3-on-3 α-helical sandwich. Concomitantly, eukaryote and bacterial globins with a truncated 2-on-2 α-helical fold were discovered. Genomic information over the last 20 years has dramatically expanded the list of known globins, demonstrating their existence in a limited number of archaeal genomes, a majority of bacterial genomes and an overwhelming majority of eukaryote genomes. In vertebrates, 6 additional globin types were identified, namely neuroglobin (Ngb), cytoglobin (Cygb), globin E (GbE), globin X (GbX), globin Y (GbY) and androglobin (Adgb). Furthermore, functions beyond the familiar oxygen transport and storage have been discovered within the vertebrate globin family, including NO metabolism, peroxidase activity, scavenging of free radicals, and signaling functions. The extension of the knowledge on globin functions suggests that the original roles of bacterial globins must have been enzymatic, involved in defense against NO toxicity, and perhaps also as sensors of O 2 , regulating taxis away or towards high O 2 concentrations. In this review, we aimed to discuss the evolution and remarkable functional diversity of vertebrate globins with particular focus on the variety of non-canonical expression sites of mammalian globins and their according impressive variability of atypical functions.

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Section: Vertebrate Globinsmentioning

confidence: 99%

Lessons from the post-genomic era: Globin diversity beyond oxygen binding and transport

et al. 2020

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“…The haemoglobin gene family has also been under strong selective pressure in notothenioids 56 . Haemoglobin is essential for oxygen transport, and the evolution of haemoglobin genes has been fuelled by duplications that enabled diversification of paralogous genes, as well as adaptation to changing environments through alterations in expression patterns 57,58 . In teleosts, haemoglobins are organised in two clusters, each containing both α and β globin genes: the larger MN cluster (flanked by genes mpg and nprl3 ), and the smaller LA cluster (flanked by lcmt1 and aqp8 ) 59 .…”

Section: Introductionmentioning

confidence: 99%

Genomics of cold adaptations in the Antarctic notothenioid fish radiation

Bista

Wood

Desvignes

et al. 2022

Preprint

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Numerous novel adaptations characterise the radiation of notothenioids, the dominant fish group in the freezing seas of the Southern Ocean. To improve understanding of the evolution of this iconic fish group, we generated and analysed new genome assemblies for 24 species covering all major subgroups of the radiation. We present a new estimate for the onset of the radiation at 10.7 million years ago, based on a time-calibrated phylogeny derived from genome-wide sequence data. We identify a two-fold variation in genome size, driven by expansion of multiple transposable element families, and use long-read sequencing data to reconstruct two evolutionarily important, highly repetitive gene family loci. First, we present the most complete reconstruction to date of the antifreeze glycoprotein gene family, whose emergence enabled survival in sub-zero temperatures, showing the expansion of the antifreeze gene locus from the ancestral to the derived state. Second, we trace the loss of haemoglobin genes in icefishes, the only vertebrates lacking functional haemoglobins, through complete reconstruction of the two haemoglobin gene clusters across notothenioid families. Finally, we show that both the haemoglobin and antifreeze genomic loci are characterised by multiple transposon expansions that may have driven the evolutionary history of these genes.

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“…Whereas the loss of erythrocytes among vertebrates is unique to icefishes, many closely related, but red-blooded, cryonotothenioid species cohabit the SO. Although having erythrocytes, these red-blooded species show a phylogenetic trend toward reduced hematocrit and/or mean corpuscular hemoglobin concentration, decreased hemoglobin multiplicity, and lowered hemoglobin affinity for O 2 as one proceeds from basal clades to the crown group Channichthyidae [1][2][3][4]. Intriguingly, several red-blooded Antarctic notothenioids survive experimentally induced anemia.…”

Section: Introductionmentioning

confidence: 99%

Developmental constraint shaped genome evolution and erythrocyte loss in Antarctic fishes following paleoclimate change

et al. 2020

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In the frigid, oxygen-rich Southern Ocean (SO), Antarctic icefishes (Channichthyidae; Notothenioidei) evolved the ability to survive without producing erythrocytes and hemoglobin, the oxygen-transport system of virtually all vertebrates. Here, we integrate paleoclimate records with an extensive phylogenomic dataset of notothenioid fishes to understand the evolution of trait loss associated with climate change. In contrast to buoyancy adaptations in this clade, we find relaxed selection on the genetic regions controlling erythropoiesis evolved only after sustained cooling in the SO. This pattern is seen not only within icefishes but also occurred independently in other high-latitude notothenioids. We show that one species of the red-blooded dragonfish clade evolved a spherocytic anemia that phenocopies human patients with this disease via orthologous mutations. The genomic imprint of SO climate change is biased toward erythrocyte-associated conserved noncoding elements (CNEs) rather than to coding regions, which are largely preserved through pleiotropy. The drift in CNEs is specifically enriched near genes that are preferentially expressed late in erythropoiesis. Furthermore, we find that the hematopoietic marrow of icefish species retained proerythroblasts, which indicates that early erythroid development remains intact. Our results provide a framework for understanding the interactions between development and the genome in shaping the response of species to climate change.

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Adaptations to environmental change: Globin superfamily evolution in Antarctic fishes

Cited by 11 publications

References 172 publications

Lessons from the post-genomic era: Globin diversity beyond oxygen binding and transport

Lessons from the post-genomic era: Globin diversity beyond oxygen binding and transport

Genomics of cold adaptations in the Antarctic notothenioid fish radiation

Developmental constraint shaped genome evolution and erythrocyte loss in Antarctic fishes following paleoclimate change

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