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De Novo Gene Evolution of Antifreeze Glycoproteins in Codfishes Revealed by Whole Genome Sequence Data

Baalsrud, Helle Tessand, Tørresen, Ole Kristian, Solbakken, Monica Hongrø, Salzburger, Walter, Hanel, Reinhold, Jakobsen, Kjetill S, Jentoft, Sissel·2018·Molecular Biology and Evolution
DOI 10.1093/molbev/msx311PMC PMC5850335
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Fig. 1. afgps in codfishes. (A) Gene organization of afgps in G. morhua and M. aeglefinus. The afgp genes have been divided up in promoter, 5′UTR, signal peptide, intron, afgp repeat and 3′UTR and colored according to legend. The hatched yellow indicates a truncated 3′UTR. The sequences are labeled with species name, a scaffold (scf) or linkage group (LG) identifier, name of afgps with Ψ signifying a pseudogene, and the length of each gene given as number of amino acids (aa). The organization of a complete, functional afgp gene is shown with triangles indicating cleavage sites of the polyprotein peptide. (B) Presence of afgp in a selection of codfishes in a phylogenetic context, showing copy numbers of different parts of afgps mapped on a time-calibrated species tree modified from (Malmstrøm et al. 2016) with time given in millions of years (Ma). The time period when freezing temperatures appeared in the Northern Hemisphere is shaded in blue (Eastman 1997). Species shown to have functional AFGP and thermal hysteresis are denoted with (+): A. glacilis, B. saida (Praebel 2005), G. chalcogrammus (Tsuda and Miura 2005), and G. morhua (Hew et al. 1981). Species shown not to have functional AFGPs or thermal hysteresis are denoted with (–): M. aeglefinus (Ewart et al. 2000) and P. virens (Denstad et al. 1987). The numbers of putative promoters, ex2, and beginning of ex3 (containing afgp repeat) and 3′UTR are given in the colored boxes. The branches where afgps originated and pseudogenized according to the most parsimonious explanation are indicated in the tree according to the legend along with the first appearance of an afgp 5′UTR sequence.
Fig. 1. afgps in codfishes. (A) Gene organization of afgps in G. morhua and M. aeglefinus. The afgp genes have been divided up in promoter, 5′UTR, signal peptide, intron, afgp repeat and 3′UTR and colored according to legend. The hatched yellow indicates a truncated 3′UTR. The sequences are labeled with species name, a scaffold (scf) or linkage group (LG) identifier, name of afgps with Ψ signifying a pseudogene, and the length of each gene given as number of amino acids (aa). The organization of a complete, functional afgp gene is shown with triangles indicating cleavage sites of the polyprotein peptide. (B) Presence of afgp in a selection of codfishes in a phylogenetic context, showing copy numbers of different parts of afgps mapped on a time-calibrated species tree modified from (Malmstrøm et al. 2016) with time given in millions of years (Ma). The time period when freezing temperatures appeared in the Northern Hemisphere is shaded in blue (Eastman 1997). Species shown to have functional AFGP and thermal hysteresis are denoted with (+): A. glacilis, B. saida (Praebel 2005), G. chalcogrammus (Tsuda and Miura 2005), and G. morhua (Hew et al. 1981). Species shown not to have functional AFGPs or thermal hysteresis are denoted with (–): M. aeglefinus (Ewart et al. 2000) and P. virens (Denstad et al. 1987). The numbers of putative promoters, ex2, and beginning of ex3 (containing afgp repeat) and 3′UTR are given in the colored boxes. The branches where afgps originated and pseudogenized according to the most parsimonious explanation are indicated in the tree according to the legend along with the first appearance of an afgp 5′UTR sequence.CC BY-NC · PubMed Central
Fig. 2. Phylogeny of afgps and afgp-like sequences in codfishes. Sequences from the genomes of G. morhua, M. aeglefinus, G. chalcogrammus, B. saida, A. glacilis, M. merlangius, P. virens, T. minutus, and G. argenteus are included. The sequences from G. morhua and M. aeglefinus have a scaffold (scf) or linkage group (LG) identifier and sequence annotation (either afgp or afgp-like). Ψ is signifying a pseudogene. The remaining sequences have an assigned letter following the species name (details regarding content and genomic position of each sequence is given in supplementary table S3, Supplementary Material online). The tree topology was constructed with MrBayes. Posterior probabilities are shown for the main branching patterns in addition to bootstrap support for a maximum likelihood topology (using MEGA 7). Putatively functional afgps and afgp-like sequences are highlighted in blue and green, respectively, according to legend.
Fig. 2. Phylogeny of afgps and afgp-like sequences in codfishes. Sequences from the genomes of G. morhua, M. aeglefinus, G. chalcogrammus, B. saida, A. glacilis, M. merlangius, P. virens, T. minutus, and G. argenteus are included. The sequences from G. morhua and M. aeglefinus have a scaffold (scf) or linkage group (LG) identifier and sequence annotation (either afgp or afgp-like). Ψ is signifying a pseudogene. The remaining sequences have an assigned letter following the species name (details regarding content and genomic position of each sequence is given in supplementary table S3, Supplementary Material online). The tree topology was constructed with MrBayes. Posterior probabilities are shown for the main branching patterns in addition to bootstrap support for a maximum likelihood topology (using MEGA 7). Putatively functional afgps and afgp-like sequences are highlighted in blue and green, respectively, according to legend.CC BY-NC · PubMed Central
Fig. 3. Synteny of genes flanking afgp and tryps in codfishes and notothenioids. Scaffold (scf), linkage group (LG), or chromosome (chr) is specified under each species, orientation of genes is indicated as arrows, grey triangles denote unidentified ORFs and truncated lines indicate regions containing genes not shown for practical purposes. (A) Synteny of the afgp genomic region in G. morhua (gadMor2) and M. aeglefinus (melAeg) compared with the following teleosts lacking afgps: G. aculeatus, T. nigroviridis, T. rubripes, O. niloticus, X. maculates, and E. lucius. Scf9468 in G. morhua has been placed in a gap in LG06 based on syntenic context and overlap at the afgp locus. (B) Genomic organization of the afgp locus in N. coriiceps. (C) Synteny of the trypsinogen locus in N. coriiceps and G. aculeatus, T. nigroviridis, T. rubripes, O. niloticus, and E. lucius.
Fig. 3. Synteny of genes flanking afgp and tryps in codfishes and notothenioids. Scaffold (scf), linkage group (LG), or chromosome (chr) is specified under each species, orientation of genes is indicated as arrows, grey triangles denote unidentified ORFs and truncated lines indicate regions containing genes not shown for practical purposes. (A) Synteny of the afgp genomic region in G. morhua (gadMor2) and M. aeglefinus (melAeg) compared with the following teleosts lacking afgps: G. aculeatus, T. nigroviridis, T. rubripes, O. niloticus, X. maculates, and E. lucius. Scf9468 in G. morhua has been placed in a gap in LG06 based on syntenic context and overlap at the afgp locus. (B) Genomic organization of the afgp locus in N. coriiceps. (C) Synteny of the trypsinogen locus in N. coriiceps and G. aculeatus, T. nigroviridis, T. rubripes, O. niloticus, and E. lucius.CC BY-NC · PubMed Central
Fig. 4. ISD for all genes in the G. morhua genome assembly. A histograms of the distribution of mean ISD for all annotated genes in G. morhua with the average mean ISD for afgp is shown. Average mean ISD for all genes in the G. morhua genome assembly was 0.36. ISD was calculated using IUPred for each amino acid position in each annotated gene in G. morhua.
Fig. 4. ISD for all genes in the G. morhua genome assembly. A histograms of the distribution of mean ISD for all annotated genes in G. morhua with the average mean ISD for afgp is shown. Average mean ISD for all genes in the G. morhua genome assembly was 0.36. ISD was calculated using IUPred for each amino acid position in each annotated gene in G. morhua.CC BY-NC · PubMed Central
Fig. 5. afgp, afpp, tlp, tryps1, and tryps3 in notothenioids. Copy numbers of the different genes mapped on a phylogeny modified from (Colombo et al. 2015) and reprinted with permission. Time is given in millions of years (Ma). Species shown to have functional AFGP and thermal hysteresis are signified by (+): P. antarctica (Wöhrmann 1995), D. mawsoni, G. acuticeps (Cheng et al. 2006), T. newnesi (Fields and Devries 2015), N. coriiceps, C. aceratus (DeVries 1971), Harpagifer spp., A. skottsbergi (Miya et al. 2016) and species shown not to have functional AFGPs or thermal hysteresis are signified by (–): E. maclovinus (Cheng 2003), P. guntheri (Miya et al. 2016). The branches with origin and losses of afgp and afpp, that gives the most parsimonious explanation of the occurrence of the events, are indicated as shown in legend, together with the onset of the Antarctic circumpolar current (ACC) and freezing temperatures in the Antarctic (Eastman 1997). Presence of afpp in D. mawsoni is unknown. Copy numbers in D. mawsoni are taken from Nicodemus-Johnson et al. (2011) and N. coriiceps genome assembly was generated by Shin et al. (2014). H. kerguelensis is inserted in the place of its sister species Harpagifer antarcticus (Derome et al. 2002).
Fig. 5. afgp, afpp, tlp, tryps1, and tryps3 in notothenioids. Copy numbers of the different genes mapped on a phylogeny modified from (Colombo et al. 2015) and reprinted with permission. Time is given in millions of years (Ma). Species shown to have functional AFGP and thermal hysteresis are signified by (+): P. antarctica (Wöhrmann 1995), D. mawsoni, G. acuticeps (Cheng et al. 2006), T. newnesi (Fields and Devries 2015), N. coriiceps, C. aceratus (DeVries 1971), Harpagifer spp., A. skottsbergi (Miya et al. 2016) and species shown not to have functional AFGPs or thermal hysteresis are signified by (–): E. maclovinus (Cheng 2003), P. guntheri (Miya et al. 2016). The branches with origin and losses of afgp and afpp, that gives the most parsimonious explanation of the occurrence of the events, are indicated as shown in legend, together with the onset of the Antarctic circumpolar current (ACC) and freezing temperatures in the Antarctic (Eastman 1997). Presence of afpp in D. mawsoni is unknown. Copy numbers in D. mawsoni are taken from Nicodemus-Johnson et al. (2011) and N. coriiceps genome assembly was generated by Shin et al. (2014). H. kerguelensis is inserted in the place of its sister species Harpagifer antarcticus (Derome et al. 2002).CC BY-NC · PubMed Central

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Research works printed but not linked: 59

  1. Albà, 2007, On homology searches by protein Blast and the characterization of the age of genes, BMC Evol Biol., 7, 53, 10.1186/1471-2148-7-53 · DOI
  2. Altschul, 1990, Basic local alignment search tool, J Mol Biol, 215, 403, 10.1016/S0022-2836(05)80360-2 · DOI · Paper page
  3. Bao, 2015, Repbase update, a database of repetitive elements in eukaryotic genomes, Mob DNA, 6, 462, 10.1186/s13100-015-0041-9 · DOI
  4. Bildanova, 2013, Main properties and evolutionary features of antifreeze proteins, Russ J Genet Appl Res., 3, 66, 10.1134/S207905971301005X · DOI
  5. Cao, 2016, Neofunctionalization of zona pellucida proteins enhances freeze-prevention in the eggs of Antarctic notothenioids, Nat Comms., 7, 10.1038/ncomms12987 · DOI
  6. Carvunis, 2012, Proto-genes and de novo gene birth, Nature, 487, 370, 10.1038/nature11184 · DOI · Paper page
  7. Cheng, 1999, Evolution of an antifreeze glycoprotein, Nature, 401, 443, 10.1038/46721 · DOI
  8. Cheng, 1998, Evolution of the diverse antifreeze proteins, Curr Opin Genet Dev., 8, 715, 10.1016/S0959-437X(98)80042-7 · DOI
  9. Cheng, 2003, Functional antifreeze glycoprotein genes in temperate-water New Zealand Nototheniid fish infer an antarctic evolutionary origin, Mol Biol Evol., 20, 1897, 10.1093/molbev/msg208 · DOI
  10. Cheng, 2006, Nonhepatic origin of notothenioid antifreeze reveals pancreatic synthesis as common mechanism in polar fish freezing avoidance, Proc Natl Acad Sci U S A, 103, 10491, 10.1073/pnas.0603796103 · DOI
  11. Chen, 1997, Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish, Proc Natl Acad Sci U S A, 94, 3811, 10.1073/pnas.94.8.3811 · DOI · Paper page
  12. Chen, 1997, Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod, Proc Natl Acad Sci U S A, 94, 3817, 10.1073/pnas.94.8.3817 · DOI · Paper page
  13. Colombo, 2015, Diversity and disparity through time in the adaptive radiation of Antarctic notothenioid fishes, J Evol Biol., 28, 376, 10.1111/jeb.12570 · DOI
  14. Cziko, 2014, Antifreeze protein-induced superheating of ice inside Antarctic notothenioid fishes inhibits melting during summer warming, Proc Natl Acad Sci U S A, 111, 14583, 10.1073/pnas.1410256111 · DOI
  15. Denstad, 1987, Thermal hysteresis antifreeze agents in fishes from Spitsbergen waters, Pol Res., 5, 1, 10.3402/polar.v5i2.6874 · DOI
  16. Derome, 2002, Phylogeny of Antarctic dragonfishes (Bathydraconidae, Notothenioidei, Teleostei) and related families based on their anatomy and two mitochondrial genes, Mol Phyl Evol, 24, 139, 10.1016/S1055-7903(02)00223-3 · DOI
  17. DeVries, 1971, Glycoproteins as biological antifreeze agents in Antarctic fishes, Science, 172, 1152, 10.1126/science.172.3988.1152 · DOI
  18. Dosztanyi, 2005, IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content, Bioinformatics, 21, 3433, 10.1093/bioinformatics/bti541 · DOI
  19. Eastman, 1997, Comparison of the Antarctic and Arctic fish faunas, Cybium, 21, 335
  20. Echols, 2002, Comprehensive analysis of amino acid and nucleotide composition in eukaryotic genomes, comparing genes and pseudogenes, Nucleic Acids Res., 30, 2515, 10.1093/nar/30.11.2515 · DOI
  21. Elhaik, 2005, The “Inverse Relationship Between Evolutionary Rate and Age of Mammalian Genes” is an artifact of increased genetic distance with rate of evolution and time of divergence, Mol Biol Evol., 23, 1, 10.1093/molbev/msj006 · DOI
  22. Ewart, 2000, Freeze susceptibility in haddock (Melanogrammus aeglefinus), Aquaculture, 188, 91, 10.1016/S0044-8486(00)00325-2 · DOI
  23. Ewart, 1999, Structure, function and evolution of antifreeze proteins, Cell Mol Life Sci., 55, 271, 10.1007/s000180050289 · DOI
  24. Fields, 2015, Variation in blood serum antifreeze activity of Antarctic Trematomus fishes across habitat temperature and depth, Comp Biochem Physiol, Part A Mol. Integr Physiol., 185, 43, 10.1016/j.cbpa.2015.03.006 · DOI
  25. Frazer, 2004, VISTA: computational tools for comparative genomics, Nucleic Acids Res., 32, W273, 10.1093/nar/gkh458 · DOI
  26. Goodwin, 2016, Coming of age: ten years of next-generation sequencing technologies, Nat Rev Genet., 17, 333, 10.1038/nrg.2016.49 · DOI · Paper page
  27. Graham, 2013, Helical antifreeze proteins have independently evolved in fishes on four occasions, PLoS ONE, 8, e81285., 10.1371/journal.pone.0081285 · DOI
  28. Gupta, 2014, Antifreeze proteins enable plants to survive in freezing conditions, J Biosci., 39, 931, 10.1007/s12038-014-9468-2 · DOI
  29. Harding, 2003, “Antifreeze” glycoproteins from polar fish, Eur J Biochem., 270, 1381, 10.1046/j.1432-1033.2003.03488.x · DOI
  30. Hew, 1981, Antifreeze glycoproteins in the plasma of Newfoundland Atlantic cod (Gadus morhua), Can J Zool, 59, 2186, 10.1139/z81-296 · DOI
  31. Kennett, 1977, Cenozoic evolution of antarctic glaciation, circum-antarctic ocean, and their impact on global paleoceanography, J Geophys Res Oceans, 82, 3843, 10.1029/JC082i027p03843 · DOI
  32. Khalturin, 2009, More than just orphans: are taxonomically-restricted genes important in evolution?, Trends Genet., 25, 404, 10.1016/j.tig.2009.07.006 · DOI
  33. Kristiansen, 2005, The mechanism by which fish antifreeze proteins cause thermal hysteresis, Cryobiology, 51, 262, 10.1016/j.cryobiol.2005.07.007 · DOI
  34. Kumar, 2016, MEGA7: Molecular Evolutionary Genetics Analysis Version 7.0 for Bigger Datasets, Mol Biol Evol., 33, 1870, 10.1093/molbev/msw054 · DOI
  35. Liu, 2007, Structure and evolutionary origin of Ca2+-dependent herring Type II antifreeze protein, PLoS ONE, 2, e548, 10.1371/journal.pone.0000548 · DOI
  36. Malmstrøm, 2017, Whole genome sequencing data and de novo draft assemblies for 66 teleost species, Sci Data, 4, 1–13., 10.1038/sdata.2016.132 · DOI
  37. Malmstrøm, 2016, Evolution of the immune system influences speciation rates in teleost fishes, Nat Genet., 48, 1204, 10.1038/ng.3645 · DOI
  38. Masel, 2006, Cryptic genetic variation is enriched for potential adaptations, Genetics, 172, 1985, 10.1534/genetics.105.051649 · DOI
  39. McLysaght, 2015, New genes from non-coding sequence: the role of de novo protein-coding genes in eukaryotic evolutionary innovation, Philos Trans R Soc Lond B Biol Sci., 370, 20140332, 10.1098/rstb.2014.0332 · DOI
  40. McLysaght, 2016, Open questions in the study of de novo genes: what, how and why, Nat Rev Genet., 17, 579, 10.1038/nrg.2016.78 · DOI
  41. Miller, 2008, Aggressive assembly of pyrosequencing reads with mates, Bioinformatics, 24, 2818, 10.1093/bioinformatics/btn548 · DOI
  42. Miya, 2016, Multiple independent reduction or loss of antifreeze trait in low Antarctic and sub-Antarctic notothenioid fishes, Antarct Sci., 28, 17, 10.1017/S0954102015000413 · DOI
  43. Near, 2012, Ancient climate change, antifreeze, and the evolutionary diversification of Antarctic fishes, Proc Natl Acad Sci U S A, 109, 3434, 10.1073/pnas.1115169109 · DOI
  44. Nicodemus-Johnson, 2011, Assembly of the antifreeze glycoprotein/trypsinogen-like protease genomic locus in the Antarctic toothfish Dissostichus mawsoni (Norman), Genomics, 98, 194, 10.1016/j.ygeno.2011.06.002 · DOI
  45. Praebel, 2005, Antifreeze activity in the gastrointestinal fluids of Arctogadus glacialis (Peters 1874) is dependent on food type, J Evol Biol., 208, 2609
  46. Romero, 1998, Thousands of proteins likely to have long disordered regions, Pac Symp Biocomput, 3, 437
  47. Rondeau, 2014, The genome and linkage map of the northern pike (Esox lucius): conserved synteny revealed between the Salmonid Sister Group and the Neoteleostei, PLoS ONE, 9, e102089, 10.1371/journal.pone.0102089 · DOI
  48. Ronquist, 2003, MrBayes 3: Bayesian phylogenetic inference under mixed models, Bioinformatics, 19, 1572, 10.1093/bioinformatics/btg180 · DOI
  49. Schlötterer, 2015, Genes from scratch—the evolutionary fate of de novo genes, Trends Genet., 31, 215, 10.1016/j.tig.2015.02.007 · DOI
  50. Shin, 2014, The genome sequence of the Antarctic bullhead notothen reveals evolutionary adaptations to a cold environment, Genome Biol., 15, 468., 10.1186/s13059-014-0468-1 · DOI
  51. Simão, 2015, BUSCO: assessing genome assembly and annotation completeness with single-copy orthologs, Bioinformatics, 31, 3210, 10.1093/bioinformatics/btv351 · DOI · Paper page
  52. Star, 2011, The genome sequence of Atlantic cod reveals a unique immune system, Nature, 477, 207, 10.1038/nature10342 · DOI · Paper page
  53. Tørresen, 2017, An improved genome assembly uncovers prolific tandem repeats in Atlantic cod, BMC Genomics, 18, 311, 10.1186/s12864-016-3448-x · DOI · Paper page
  54. Wilson, 2017, Young genes are highly disordered as predicted by the preadaptation hypothesis of de novo gene birth, Nat Ecol Evol., 1, 0146–0146., 10.1038/s41559-017-0146 · DOI
  55. Wilson, 2011, Putatively noncoding transcripts show extensive association with ribosomes, Genome Biol Evol., 3, 1245, 10.1093/gbe/evr099 · DOI
  56. Wöhrmann, 1995, Antifreeze glycopeptides of the high-Antarctic silverfish Pleuragramma antarcticum (Notothenioidei), Comp Biochem Physiol C Pharmacol Toxicol Endocrinol., 111, 121, 10.1016/0742-8413(95)00007-T · DOI
  57. Yang, 2013, Chemical synthesis of a masked analogue of the fish antifreeze potentiating protein (AFPP), Org Biomol Chem., 11, 4935, 10.1039/c3ob41066h · DOI
  58. Yates, 2016, 2016. Ensembl 2016, Nucleic Acids Res., 44, D710, 10.1093/nar/gkv1157 · DOI
  59. Zhuang, 2012, Protein genes in repetitive sequence-antifreeze glycoproteins in Atlantic cod genome, BMC Genomics, 13, 293., 10.1186/1471-2164-13-293 · DOI · Paper page

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Authors
Baalsrud, H. T., Tørresen, O. K., Solbakken, M. H., Salzburger, W., Hanel, R., Jakobsen, K. S., & Jentoft, S.
Affiliations
  • Department of Biosciences, Centre for Ecological and Evolutionary Synthesis (CEES), University of Oslo, Oslo, Norway
  • Institute of Fisheries Ecology, Johann Heinrich von Thünen Institute, Federal Research Institute for Rural Areas, Forestry and Fisheries, Hamburg, Germany
ORCID
Solbakken, Monica Hongrø
Venue
Molecular Biology and Evolution
Publisher
Oxford University Press (OUP)
Published
2017-12-05
Volume
35
Issue
3
Pages
593-606
ISSN
  • 0737-4038
  • 1537-1719
DOI
10.1093/molbev/msx311
PMC
PMC5850335
Cited by
116
References
3
Language
en

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Baalsrud, H. T., Tørresen, O. K., Solbakken, M. H., Salzburger, W., Hanel, R., Jakobsen, K. S., & Jentoft, S. (2018). De Novo Gene Evolution of Antifreeze Glycoproteins in Codfishes Revealed by Whole Genome Sequence Data. Molecular Biology and Evolution. https://doi.org/10.1093/molbev/msx311