Phylogenetic analysis reveals wide distribution of globin X

Dröge, Jasmin; Makałowski, Wojciech

doi:10.1186/1745-6150-6-54

Cited by 18 publications

(20 citation statements)

References 23 publications

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“…The sequence analysis of GbX shows highest identity scores with neuroglobin (Ngb) (25-35%) (2,3,16) and suggests that phylogenetically they derive from the same common ancestor that diverged ∼800 million yr ago from the evolutionary branch of Hb, Mb, and cytoglobin (Cygb) (Fig. S1) (17).…”

Section: Resultsmentioning

confidence: 99%

“…The function of these proteins remains largely unknown. Globin X (GbX) is a novel globin found in fish, amphibians, and reptiles that diverged early from a common ancestor to hemoglobin (Hb) and myoglobin (Mb) (2,3), thus representing a landmark in the evolution of the globins, probably carrying out functions that were later taken over by other globins in higher vertebrates. Because six-coordinate globins have proximal and distal histidines that bind the heme iron and are expressed at low concentrations, it has been hypothesized that they did not evolve for oxygen storage and transport, but rather participate in reactive oxygen and nitrogen species metabolism or other processes (1,4).…”

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confidence: 99%

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Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells

Cortí

Xue

Tejero

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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The discovery of novel globins in diverse organisms has stimulated intense interest in their evolved function, beyond oxygen binding. Globin X (GbX) is a protein found in fish, amphibians, and reptiles that diverged from a common ancestor of mammalian hemoglobins and myoglobins. Like mammalian neuroglobin, GbX was first designated as a neuronal globin in fish and exhibits six-coordinate heme geometry, suggesting a role in intracellular electron transfer reactions rather than oxygen binding. Here, we report that GbX to our knowledge is the first six-coordinate globin and the first globin protein apart from hemoglobin, found in vertebrate RBCs. GbX is present in fish erythrocytes and exhibits a nitrite reduction rate up to 200-fold faster than human hemoglobin and up to 50-fold higher than neuroglobin or cytoglobin. Deoxygenated GbX reduces nitrite to form nitric oxide (NO) and potently inhibits platelet activation in vitro, to a greater extent than hemoglobin. Fish RBCs also reduce nitrite to NO and inhibit platelet activation to a greater extent than human RBCs, whereas GbX knockdown inhibits this nitrite-dependent NO signaling. The description of a novel, sixcoordinate globin in RBCs with dominant electron transfer and nitrite reduction functionality provides new insights into the evolved signaling properties of ancestral heme-globins.nitrite | nitric oxide | blood | RBC | platelet

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells

Cortí

Xue

Tejero

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…The globin X ( GbX ) gene has been documented in the genomes of some cyclostomes, elasmobranchs, teleost fishes, amphibians, and reptiles (Dröge and Makalowski 2011; Roesner et al 2005). This gene encodes a membrane-bound, hexacoordinate globin that appears to perform an antioxidant function (Blank et al 2011b).…”

Section: The Functional Diversification Of Vertebrate Globinsmentioning

confidence: 99%

Gene duplication, genome duplication, and the functional diversification of vertebrate globins

Storz

Opazo

Hoffmann

2013

Molecular Phylogenetics and Evolution

105

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The functional diversification of the vertebrate globin gene superfamily provides an especially vivid illustration of the role of gene duplication and whole-genome duplication in promoting evolutionary innovation. For example, key globin proteins that evolved specialized functions in various aspects of oxidative metabolism and oxygen signaling pathways (hemoglobin [Hb], myoglobin [Mb], and cytoglobin [Cygb]) trace their origins to two whole-genome duplication events in the stem lineage of vertebrates. The retention of the proto-Hb and Mb genes in the ancestor of jawed vertebrates permitted a physiological division of labor between the oxygen-carrier function of Hb and the oxygen-storage function of Mb. In the Hb gene lineage, a subsequent tandem gene duplication gave rise to the proto α- and β-globin genes, which permitted the formation of multimeric Hbs composed of unlike subunits (α2β2). The evolution of this heteromeric quaternary structure was central to the emergence of Hb as a specialized oxygen-transport protein because it provided a mechanism for cooperative oxygen-binding and allosteric regulatory control. Subsequent rounds of duplication and divergence have produced diverse repertoires of α- and β-like globin genes that are ontogenetically regulated such that functionally distinct Hb isoforms are expressed during different stages of prenatal development and postnatal life. In the ancestor of jawless fishes, the proto Mb and Hb genes appear to have been secondarily lost, and the Cygb homolog evolved a specialized respiratory function in blood-oxygen transport. Phylogenetic and comparative genomic analyses of the vertebrate globin gene superfamily have revealed numerous instances in which paralogous globins have convergently evolved similar expression patterns and/or similar functional specializations in different organismal lineages.

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“…The most recent molecular phylogenetic analysis of globin sequences from the five □ S This article contains supplemental (19) demonstrated that the functional hexacoordinated Globin X (GbX) protein of the cypriniform adult zebrafish is located in the nervous central system and retina, suggesting a neural-based function but contradicting a previous result obtained from the other cypriniform Carassius auratus GbX showing that mRNA GbX was not detected in brain and eye but in other tissues (muscle, heart, gut, and liver) (20). Thought to be restricted to vertebrate, GbX-like sequences have been recently identified in silico in other deuterostomes and in protostomes, supporting an early emergence of this gene family in metazoan evolution (21).…”

mentioning

confidence: 99%

Neuroglobins, Pivotal Proteins Associated with Emerging Neural Systems and Precursors of Metazoan Globin Diversity

Lechauve

Jager

Laguerre

et al. 2013

Journal of Biological Chemistry

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Background: Neuroglobins are expressed in vertebrate neurons. Results: Neuroglobins are located in neural systems of two basal animals (acoels and jellyfish) and are ubiquitous in metazoan transcriptomes. Conclusion: Neuroglobin was recruited in neural cell prototypes and later co-opted in hemoglobin-based blood systems. Significance: The universality of neuroglobins sheds new light on the origin and evolution of globins.

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Phylogenetic analysis reveals wide distribution of globin X

Cited by 18 publications

References 23 publications

Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells

Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells

Gene duplication, genome duplication, and the functional diversification of vertebrate globins

Neuroglobins, Pivotal Proteins Associated with Emerging Neural Systems and Precursors of Metazoan Globin Diversity

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