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G.b. Kitto - One of the best experts on this subject based on the ideXlab platform.
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Amino acid sequence of the coelomic C Globin from the sea cucumber Caudina (Molpadia) arenicola.
Journal of Protein Chemistry, 1992Co-Authors: Gene D. Mcdonald, Lois Davidson, G.b. KittoAbstract:The sequence of a Globin from a marine invertebrate, the sea cucumberCaudina (Molpadia) arenicola (Echinodermata), is reported. This Globin, chain C, is one of four major Globins found in coelomic red cells in this organism and is the second to be sequenced. Chain C consists of 157 residues, is amino-terminally acetylated, and has an extended amino-terminal region. This Globin shares a 60% sequence identity with the other sequencedC. arenicola Globin, D chain (Mauriet al., Biochem. Biophys. Acta1078, 63–67, 1991), but has a 93.6% identity with a Globin from another sea cucumber,Paracaudina chilensis (Suzuki,Biochem. Biophys. Acta,998, 292–296, 1989).
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Amino acid sequence of a Globin from the sea cucumber Caudina (Molpadia) arenicola.
Biochimica et Biophysica Acta, 1991Co-Authors: Fina Mauri, J Omnaas, Lois Davidson, C Whitfill, G.b. KittoAbstract:Abstract Coelomic cells from the sea cucumber Caudina (Molpadia) arenicola contain four major Globins, A, B, C and D. The hemoGlobins from this organism show unusual ligand-linked dissociation properties. The complete amino acid sequence of the D Globin has been established. It is N-acetylated, consists of 158 residues and has a 10 amino acid N-terminal extension similar to that found in some other invertebrate Globins. The C. arenicola D Globin has an equal sequence identity (28%) with both α and β human Globins and as anticipated, is more closely related to these vertebrate proteins than are molluscan Globins. The C. arenicola D Globin shows a 59% identity with the Globin I from the sea cucumber Paracaudina chilensis. The availability of the C. arenicola D Globin sequence will aid the X-ray analysis of this protein and facilitate an understanding of the changes in subunit interactions that occur with cooperative ligand binding.
Xavier Bailly - One of the best experts on this subject based on the ideXlab platform.
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Globins in the marine Annelid Platynereis dumerilii shed new light on hemoGlobin evolution in Bilaterians
2020Co-Authors: Solene Song, Viktor V Starunov, Xavier Bailly, Christine Ruta, Annemiek Cornelissen, Pierre Kerner, Guillaume BalavoineAbstract:Background How vascular systems and their respiratory pigments evolved is still debated. While many animals present a vascular system, hemoGlobin exists as a blood pigment only in a few groups (vertebrates, annelids, a few arthropod and mollusk species). HemoGlobins are formed of Globin sub-units, belonging to multigene families, in various multimeric assemblages. It was so far unclear whether hemoGlobin families from different bilaterian groups had a common origin. Results To unravel Globin evolution in bilaterians, we studied the marine annelid Platynereis dumerilii, a species with a slow evolving genome. Platynereis exhibits a closed vascular system filled with extracellular hemoGlobin. Platynereis genome and transcriptomes reveal a family of 19 Globins, nine of which are predicted to be extracellular. Extracellular Globins are produced by specialized cells lining the vessels of the segmental appendages of the worm, serving as gills, and thus likely participate in the assembly of a previously characterized annelid-specific giant hemoGlobin. Extracellular Globin mRNAs are absent in smaller juveniles, accumulate considerably in growing and more active worms and peak in swarming adults, as the need for O2 culminates. Next, we conducted a metazoan-wide phylogenetic analysis of Globins using data from complete genomes. We establish that five Globin genes (stem Globins) were present in the last common ancestor of bilaterians. Based on these results, we propose a new nomenclature of Globins, with five clades. All five ancestral stem-Globin clades are retained in some spiralians, while some clades disappeared early in deuterostome and ecdysozoan evolution. All known bilaterian blood Globin families are grouped in a single clade (clade I) together with intracellular Globins of bilaterians devoid of red blood. Conclusions We uncover a complex “pre-blood” evolution of Globins, with an early gene radiation in ancestral bilaterians. Circulating hemoGlobins in various bilaterian groups evolved convergently, presumably in correlation with animal size and activity. However, all hemoGlobins derive from a clade I Globin, or cytoGlobin, probably involved in intracellular O2 transit and regulation. The annelid Platynereis is remarkable in having a large family of extracellular blood Globins, while retaining all clades of ancestral bilaterian Globins.
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Globins and hemogenic cells in the marine annelid platynereis dumerilii shed new light on blood evolution in bilaterians
bioRxiv, 2019Co-Authors: Solene Song, Viktor V Starunov, Xavier Bailly, Christine Ruta, Annemiek Cornelissen, Pierre Kerner, Guillaume BalavoineAbstract:How vascular systems and their respiratory pigments evolved is still debated. To unravel blood evolution in Bilaterians, we studied the marine Annelid Platynereis dumerilii. Platynereis exhibits a closed vascular system filled with extracellular hemoGlobin. An exhaustive screen in Platynereis genome reveals a family of 17 Globins. Seven extracellular Globins are produced by specialized hemogenic cells lining the vessels of the segmental appendages of the worm, serving as gills. Extracellular Globins are absent in juveniles then accumulate considerably as the worm size and activity increase, culminating in swarming adults. Phylogenetic analyses with deep screenings in complete genomes establish that five Globin genes (stem Globins) were present in the last common ancestor of Bilaterians. All known Bilaterian blood Globins are derived convergently from a single presumably ubiquitously expressed, intracellular stem Globin gene. All five Globin types are retained in Platynereis, reinforcing this species status as a key slow evolving genome within Bilaterians.
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Microbial eukaryote Globins.
Advances in microbial physiology, 2013Co-Authors: Serge N Vinogradov, Xavier Bailly, Mariana Tinajero-trejo, David Roy Smith, Robert K. Poole, David HoogewijsAbstract:A bioinformatics survey of about 120 protist and 240 fungal genomes and transcriptomes revealed a broad array of Globins, representing five of the eight subfamilies identified in bacteria. Most conspicuous is the absence of protoGlobins and Globin-coupled sensors, except for a two-domain Globin in Leishmanias, that comprises a nucleotidyl cyclase domain, and the virtual absence of truncated group 3 Globins. In contrast to bacteria, co-occurrence of more than two Globin subfamilies appears to be rare in protists. Although Globins were lacking in the Apicomplexa and the Microsporidia intracellular pathogens, they occurred in the pathogenic Trypanosomatidae, Stramenopiles and certain fungi. FlavohaemoGlobins (FHbs) and related single-domain Globins occur across the protist groups. Fungi are unique in having FHbs co-occurring with sensor single-domain Globins (SSDgbs). Obligately biotrophic fungi covered in our analysis lack Globins. Furthermore, SSDgbs occur only in a heterolobosean amoeba, Naegleria and the stramenopile Hyphochytrium. Of the three subfamilies of truncated Mb-fold Globins, TrHb1s appear to be the most widespread, occurring as multiple copies in chlorophyte and ciliophora genomes, many as multidomain proteins. Although the ciliates appear to have only TrHb1s, the chlorophytes have Mb-like Globins and TrHb2s, both closely related to the corresponding plant Globins. The presently available number of protist genomes is inadequate to provide a definitive census of their Globins. Bayesian molecular analyses of single-domain 3/3 Mb-fold Globins suggest a close relationship of chlorophyte and haptophyte Globins, including choanoflagellate and Capsaspora Globins to land plant symbiotic and non-symbiotic haemoGlobins and to vertebrate neuroGlobins.
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Evolution of the Globin Gene Family in Deuterostomes: Lineage-Specific Patterns of Diversification and Attrition
Molecular Biology and Evolution, 2012Co-Authors: Federico G. Hoffmann, Xavier Bailly, Bettina Ebner, Thomas Hankeln, Serge N Vinogradov, Juan C. Opazo, David Hoogewijs, Jay F. StorzAbstract:In the Metazoa, Globin proteins display an underlying unity in tertiary structure that belies an extraordinary diversity in primary structures, biochemical properties, and physiological functions. Phylogenetic reconstructions can reveal which of these functions represent novel, lineage-specific innovations, and which represent ancestral functions that are shared with homologous Globin proteins in other eukaryotes and even prokaryotes. To date, our understanding of Globin diversity in deuterostomes has been hindered by a dearth of genomic sequence data from the Ambulacraria (echinoderms þ hemichordates), the sister group of chordates, and the phylum Xenacoelomorpha, which includes xenoturbellids, acoelomorphs, and nemertodermatids. Here, we report the results of a phylogenetic and comparative genomic analysis of the Globin gene repertoire of deuterostomes. We first characterized the Globin genes of the acorn worm, Saccoglossus kowalevskii, a representative of the phylum Hemichordata. We then integrated genomic sequence data from the acorn worm into a comprehensive analysis of conserved synteny and phylogenetic relationships among Globin genes from representatives of the eight lineages that comprise the superphylum Deuterostomia. The primary aims were 1) to unravel the evolutionary history of the Globin gene superfamily in deuterostomes and 2) to use the estimated phylogeny to gain insights into the functional evolution of deuterostome Globins. Results of our analyses indicate that the deuterostome common ancestor possessed a repertoire of at least four distinct Globin paralogs and that different subsets of these ancestral genes have been retained in each of the descendant organismal lineages. In each major deuterostome group, a different subset of ancestral precursor genes underwent lineage-specific expansions of functional diversity through repeated rounds of gene duplication and divergence. By integrating results of the phylogenetic analysis with available functional data, we discovered that circulating oxygen-transport hemoGlobins evolved independently in several deuterostome lineages and that intracellular nerve Globins evolved independently in chordates and acoelomorph worms.
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A model of Globin evolution.
Gene, 2007Co-Authors: Serge N Vinogradov, Xavier Bailly, David Hoogewijs, Kenji Mizuguchi, Sylvia Dewilde, Luc Moens, Jacques R VanfleterenAbstract:Putative Globins have been identified in 426 bacterial, 32 Archaeal and 67 eukaryote genomes. Among these sequences are the hitherto unsuspected presence of single domain sensor Globins within Bacteria, Fungi, and a Euryarchaeote. Bayesian phylogenetic trees suggest that their occurrence in the latter two groups could be the result of lateral gene transfer from Bacteria. Iterated psiblast searches based on groups of Globin sequences indicate that bacterial flavohemoGlobins are closer to metazoan Globins than to the other two lineages, the 2-over-2 Globins and the Globin-coupled sensors. Since Bacteria is the only kingdom to have all the subgroups of the three Globin lineages, we propose a working model of Globin evolution based on the assumption that all three lineages originated and evolved only in Bacteria. Although the 2-over-2 Globins and the Globin-coupled sensors recognize flavohemoGlobins, there is little recognition between them. Thus, in the first stage of Globin evolution, we favor a flavohemoGlobin-like single domain protein as the ancestral Globin. The next stage comprised the splitting off to single domain 2-over-2 and sensor-like Globins, followed by the covalent addition of C-terminal domains resulting in the chimeric flavohemoGlobins and Globin-coupled sensors. The last stage encompassed the lateral gene transfers of some members of the three Globin lineages to specific groups of Archaea and Eukaryotes.
F. Gannon - One of the best experts on this subject based on the ideXlab platform.
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Tail-to-tail orientation of the Atlantic salmon alpha- and beta-Globin genes
Journal of Molecular Evolution, 1994Co-Authors: A. Wagner, F. Deryckere, T. Mcmorrow, F. GannonAbstract:We report the cloning of a cDNA and two corresponding β-Globin genes of the Atlantic salmon ( Salmo salar L.) as well as two genes for α-Globins. Nucleotide sequence analysis of the cDNA shows that the predicted β-Globin peptide comprises 148 amino acids with a calculated molecular mass of 16,127 Da and an overall amino acid similarity of 40–50% to higher vertebrates and 60–90% to fish sequences. The study of the genomic organization of α- and β-Globin genes shows that, as is the case in Xenopus , the salmon genes are adjacent. Two sets of linked α- and β-Globin genes were isolated and restriction-enzyme polymorphisms indicate that they belong to two distinct loci, possibly as a result of the salmon tetraploidy. In each locus the α- and β-Globin genes are oriented 3′ to 3′ relative to each other with the RNA coding sequences located on opposite DNA strands. This is the first evidence for this type of arrangement found for Globin genes. Moreover, while the linkage found in salmon and Xenopus supports the hypothesis of an initial tandem duplication of a Globin ancestor gene, our results raise the question of the actual original orientation of the duplicated genes.
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Tail-to-tail orientation of the Atlantic salmon alpha- and beta-Globin genes.
Journal of Molecular Evolution, 1994Co-Authors: A. Wagner, F. Deryckere, T. Mcmorrow, F. GannonAbstract:We report the cloning of a cDNA and two corresponding beta-Globin genes of the Atlantic salmon (Salmo salar L.) as well as two genes for alpha-Globins. Nucleotide sequence analysis of the cDNA shows that the predicted beta-Globin peptide comprises 148 amino acids with a calculated molecular mass of 16,127 Da and an overall amino acid similarity of 40-50% to higher vertebrates and 60-90% to fish sequences. The study of the genomic organization of alpha- and beta-Globin genes shows that, as is the case in Xenopus, the salmon genes are adjacent. Two sets of linked alpha- and beta-Globin genes were isolated and restriction-enzyme polymorphisms indicate that they belong to two distinct loci, possibly as a result of the salmon tetraploidy. In each locus the alpha- and beta-Globin genes are oriented 3' to 3' relative to each other with the RNA coding sequences located on opposite DNA strands. This is the first evidence for this type of arrangement found for Globin genes. Moreover, while the linkage found in salmon and Xenopus supports the hypothesis of an initial tandem duplication of a Globin ancestor gene, our results raise the question of the actual original orientation of the duplicated genes.
Fina Mauri - One of the best experts on this subject based on the ideXlab platform.
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Amino acid sequence of a Globin from the sea cucumber Caudina (Molpadia) arenicola.
Biochimica et Biophysica Acta, 1991Co-Authors: Fina Mauri, J Omnaas, Lois Davidson, C Whitfill, G.b. KittoAbstract:Abstract Coelomic cells from the sea cucumber Caudina (Molpadia) arenicola contain four major Globins, A, B, C and D. The hemoGlobins from this organism show unusual ligand-linked dissociation properties. The complete amino acid sequence of the D Globin has been established. It is N-acetylated, consists of 158 residues and has a 10 amino acid N-terminal extension similar to that found in some other invertebrate Globins. The C. arenicola D Globin has an equal sequence identity (28%) with both α and β human Globins and as anticipated, is more closely related to these vertebrate proteins than are molluscan Globins. The C. arenicola D Globin shows a 59% identity with the Globin I from the sea cucumber Paracaudina chilensis. The availability of the C. arenicola D Globin sequence will aid the X-ray analysis of this protein and facilitate an understanding of the changes in subunit interactions that occur with cooperative ligand binding.
George P. Patrinos - One of the best experts on this subject based on the ideXlab platform.
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Mutation screening in the human ε‐Globin gene using single‐strand conformation polymorphism analysis
American Journal of Hematology, 2006Co-Authors: Adamantia Papachatzopoulou, Panagiotis G. Menounos, Christina Kolonelou, George P. PatrinosAbstract:The human e-Globin gene is necessary for primitive human erythropoiesis in the yolk sac. Herein we report a non-radioactive single-strand conformation polymorphism (SSCP) approach to screen the human e-Globin gene and its regulatory regions for possible mutations and single-nucleotide polymorphisms in normal adult subjects, in order to determine those genomic regions, which are not necessary for its proper regulation and function. We identified no sequence variations apart from the expected 5 0 e/HincII polymorphism in the fragments analyzed, suggesting that genomic alterations in the eGlobin gene are most likely incompatible with normal erythropoiesis and proper embryonic development. Am. J. Hematol. 81:136–138, 2006. a 2006 Wiley-Liss, Inc.
