Molecular cloning and sequence analysis of α- and β-globin cDNAs from yellowtail, Seriola quinqueradiata

Okamoto, Kazuyoshi; Sakai, Masahiro; Miyata, Masato

doi:10.1016/s1096-4959(01)00427-4

Cited by 9 publications

(7 citation statements)

References 27 publications

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“…In this study, we identified two types of α‐ (25 clones) and β‐ (18 clones) globin genes (Table 1). Okamoto, Sakai & Miyata (2001) reported that the homology of yellowtail α‐globin genes are most closely related to goldfish Carassius auretus (Rodewald and Braunitzer) and β‐gobin to maruadsi Decapterus maruadsi (Temminck and Schlegel) respectively.…”

Section: Resultsmentioning

confidence: 99%

Analysis of expressed sequence tags from a yellowtail, Seriola quinqueradiata (Temminck & Schlegel), head kidney cDNA library

Kono

Okamoto

Sakai

2002

Aquaculture Research

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We generated 436 expressed sequence tags (EST) from a Yellowtail, Seriola quinqueradiata (Temminck & Schlegel), kidney cDNA library. Of these, 233 EST (53.4%) showed no homology to known genes, while 203 EST (46.6%) showed homology to known genes and transcripts. Bio-defence-related cDNAs identified from kidney were ikaros, an immunogloblin light chain and several heat shock proteins. Of the other related EST, 57 were homologous to 27 different ribosomal-related proteins and rRNA genes, 2 different mitochondrial genes and the remaining 77 encoded 36 different identified genes.

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Section: Resultsmentioning

confidence: 99%

Analysis of expressed sequence tags from a yellowtail, Seriola quinqueradiata (Temminck & Schlegel), head kidney cDNA library

Kono

Okamoto

Sakai

2002

Aquaculture Research

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“…The α 2-globin had one Gly insertion at position 48. However, Yellowtail α -globin type B has a Gly insertion at position 47 [ 32 , 33 ]. Miyata et al [ 33 ] suggested that an insertion of Arg or Asp residue at position 47 in carp α -globin produced only inconsequential changes in function and the three-dimensional structure of globin.…”

Section: Discussionmentioning

confidence: 99%

“…We isolated two β -globin genes in flounder, and the deduced amino acid sequences were 98.6% homologous, and considerably homologous with other vertebrate β -globins. Both types of flounder β -globin had a Phe residue at position 121, in contrast to a Lys residue in yellowtail β -globins, when compared with human β -globin [ 32 ]. Yoshizaki et al [ 34 ] suggested that such a residue insertion may affect the function of β -globin.…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization and Expression of α‐Globin and β‐Globin Genes in the Euryhaline Flounder (Platichthys flesus)

Mayolle

Cui

et al. 2011

Evidence-Based Complementary and Alternative Medicine

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In order to understand the possible role of globin genes in fish salinity adaptation, we report the molecular characterization and expression of all four subunits of haemoglobin, and their response to salinity challenge in flounder. The entire open reading frames of α1-globin and α2-globin genes were 432 and 435 bp long, respectively, whereas the β1-globin and β2-globin genes were both 447 bp. Although the head kidney (pronephros) is the predicted major site of haematopoiesis, real-time PCR revealed that expression of α-globin and β-globin in kidney (mesonephros) was 1.5 times higher than in head kidney. Notably, the α1-globin and β1-globin mRNA expression was higher than α2-globin and β2-globin in kidney. Expression levels of all four globin subunits were higher in freshwater- (FW-) than in seawater- (SW-)adapted fish kidney. If globins do play a role in salinity adaptation, this is likely to be more important in combating the hemodilution faced by fish in FW than the dehydration and salt loading which occur in SW.

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“…The first is the hemoglobin b-chain of tilapia (Swiss-Prot accession # P83761), which has a N-terminal sequence resembling that of the Rio Grande perch (Cichlasoma cyanoguttatum: VEWTDAERKAIAGI; Gillen and Riggs 1973) and of the Japanese amberjack (Seriola quinqueradiata: MVDWTDAERAAISSL; Okamoto et al 2001) to an equal extend, and these three are all Perciform fishes. The second is the N-terminal sequence for histone H2B of carp (Swiss-Prot accession # P83837), which in comparison with sea trout (Kootstra and Bailey 1978) demonstrates a deletion between S12 and T17.…”

Section: Amino Acid Sequencementioning

confidence: 99%

Extranuclear Histones in Teleost Gills: An Evolutionary Study

Stekhoven

Bonga

Flik

2004

Fish Physiol Biochem

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Extranuclear histones and histone fragments (13-15 kDa) in gill microsomes of a phylogenetic series of teleostean fishes (tilapia, trout, carp, eel and elephant fish) were studied. Histones H2A and H2B are the first occurring of these antimicrobial agents. Halfway the evolution of teleosts (carp, trout) H3 fragments emerge, which disappear in later stages of development and are replaced by truncated H1 (tilapia). The hypothesis is forwarded that variation in composition of extranuclear histones is caused by changes in specificity of histone transporters.

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Molecular cloning and sequence analysis of α- and β-globin cDNAs from yellowtail, Seriola quinqueradiata

Cited by 9 publications

References 27 publications

Analysis of expressed sequence tags from a yellowtail, Seriola quinqueradiata (Temminck & Schlegel), head kidney cDNA library

Analysis of expressed sequence tags from a yellowtail, Seriola quinqueradiata (Temminck & Schlegel), head kidney cDNA library

Molecular Characterization and Expression of α‐Globin and β‐Globin Genes in the Euryhaline Flounder (Platichthys flesus)

Extranuclear Histones in Teleost Gills: An Evolutionary Study

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