Hemoglobin Kawachi [α44 (CE2) Pro → Arg] : A new Hemoglobin Variant of High Oxygen Affinity with Amino Acid Substitution at α<sub>1</sub>β<sub>2</sub>Contact

Harano, Teruo; Harano, Keiko; Ueda, Seinosuke; Shibata, Susumu; Imai, Katsunori; Ohba, Yusuke; Shinohara, T; Horio, S.; Nishioka, Kazuhiro; Shirotani, Hitoshi

doi:10.3109/03630268208996932

Cited by 20 publications

(3 citation statements)

References 15 publications

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“…This steric hindrance renders the T-state of guinea pig hemoglobin less stable and therefore will result in a higher oxygen affinity since the equilibrium between T-, R- and R2-state will be shifted towards the relaxed states (either R- or R2-state), which have a higher oxygen affinity. Human hemoglobin mutants confirm this hypothesis, since the mutants Milledgeville (Pro44Leu) and Kawachi (Pro44Arg) have a strongly increased oxygen affinity [33], [34]. This may explain why Pro44 of the α-subunit is highly conserved in vertebrate hemoglobin.…”

Section: Resultsmentioning

confidence: 78%

Structure of the Altitude Adapted Hemoglobin of Guinea Pig in the R2-State

Pairet

Jaenicke

2010

PLoS ONE

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BackgroundGuinea pigs are considered to be genetically adapted to a high altitude environment based on the consistent finding of a high oxygen affinity of their blood.Methodology/Principal FindingsThe crystal structure of guinea pig hemoglobin at 1.8 Å resolution suggests that the increased oxygen affinity of guinea pig hemoglobin can be explained by two factors, namely a decreased stability of the T-state and an increased stability of the R2-state. The destabilization of the T-state can be related to the substitution of a highly conserved proline (P44) to histidine (H44) in the α-subunit, which causes a steric hindrance with H97 of the β-subunit in the switch region. The stabilization of the R2-state is caused by two additional salt bridges at the β1/β2 interface.Conclusions/SignificanceBoth factors together are supposed to serve to shift the equilibrium between the conformational states towards the high affinity relaxed states resulting in an increased oxygen affinity.

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Section: Resultsmentioning

confidence: 78%

Structure of the Altitude Adapted Hemoglobin of Guinea Pig in the R2-State

Pairet

Jaenicke

2010

PLoS ONE

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“…Our study revealed a very strong differentiation of the polymorphic HbαD subunit when comparing wild vs farm populations. We predict that the Thr44 variant identified in farm1 and farm3 increases the oxygen binding affinity similar to the human hemoglobin Kawachi (Pro44α → Arg) variant 103 of importance during hypoxic conditions.…”

Section: Discussionmentioning

confidence: 94%

Non-synonymous variation and protein structure of candidate genes associated with selection in farm and wild populations of turbot (Scophthalmus maximus)

Andersen

Rubiolo

Pirolli³

et al. 2023

Sci Rep

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Non-synonymous variation (NSV) of protein coding genes represents raw material for selection to improve adaptation to the diverse environmental scenarios in wild and livestock populations. Many aquatic species face variations in temperature, salinity and biological factors throughout their distribution range that is reflected by the presence of allelic clines or local adaptation. The turbot (Scophthalmus maximus) is a flatfish of great commercial value with a flourishing aquaculture which has promoted the development of genomic resources. In this study, we developed the first atlas of NSVs in the turbot genome by resequencing 10 individuals from Northeast Atlantic Ocean. More than 50,000 NSVs where detected in the ~ 21,500 coding genes of the turbot genome, and we selected 18 NSVs to be genotyped using a single Mass ARRAY multiplex on 13 wild populations and three turbot farms. We detected signals of divergent selection on several genes related to growth, circadian rhythms, osmoregulation and oxygen binding in the different scenarios evaluated. Furthermore, we explored the impact of NSVs identified on the 3D structure and functional relationship of the correspondent proteins. In summary, our study provides a strategy to identify NSVs in species with consistently annotated and assembled genomes to ascertain their role in adaptation.

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“…Arg) were both associated with increased oxygen affinity, and the former was associated with mild erythrocytosis as well. [6,7] The corresponding CCG ! GCG mutation at a2 codon 44 has been independently identified by H. This variant was identified in a 31-year-old, apparently healthy, Arab woman of Yemen, who was living in Buffalo, NY, USA.…”

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confidence: 99%

THREE NEW VARIANTS OF THEα1-GLOBIN GENE WITHOUT CLINICAL OR HEMATOLOGIC EFFECTS: Hb HAGERSTOWN [α44(CE2)Pro→Ala (α1)]; Hb BUFFALO [α89(FG1)His→Gln (α1)], A HEMOGLOBIN VARIANT FROM SOMALIA AND YEMEN; Hb WICHITA [α95(G2)Pro→Gln (α1)]; AND A SECOND, UNRELATED, CASE OF Hb ROUBAIX [α55(E4)Val→Leu (α1)]

et al. 2002

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Hemoglobin Kawachi [α44 (CE2) Pro → Arg] : A new Hemoglobin Variant of High Oxygen Affinity with Amino Acid Substitution at α₁β₂Contact

Cited by 20 publications

References 15 publications

Structure of the Altitude Adapted Hemoglobin of Guinea Pig in the R2-State

Structure of the Altitude Adapted Hemoglobin of Guinea Pig in the R2-State

Non-synonymous variation and protein structure of candidate genes associated with selection in farm and wild populations of turbot (Scophthalmus maximus)

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Hemoglobin Kawachi [α44 (CE2) Pro → Arg] : A new Hemoglobin Variant of High Oxygen Affinity with Amino Acid Substitution at α1β2Contact

Cited by 20 publications

References 15 publications

Structure of the Altitude Adapted Hemoglobin of Guinea Pig in the R2-State

Structure of the Altitude Adapted Hemoglobin of Guinea Pig in the R2-State

Non-synonymous variation and protein structure of candidate genes associated with selection in farm and wild populations of turbot (Scophthalmus maximus)

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Hemoglobin Kawachi [α44 (CE2) Pro → Arg] : A new Hemoglobin Variant of High Oxygen Affinity with Amino Acid Substitution at α₁β₂Contact