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ABSTRACT Cave‐dwelling animals thrive in isolated caves despite the pressures of darkness, starvation, and reduced oxygen. Prior work revealed thatAstyanaxcave‐dwelling morphs derived from different cave localities express significantly higher levels of blood hemoglobin compared to surface‐dwelling fish. Interestingly, this elevation is maintained in different populations of cavefish, despite captive rearing in normal oxygen conditions. We capitalized on the consistent response of elevated hemoglobin in captive cavefish, which were derived from geographically distinct regions, to determine if this elevation is underpinned by expression of the sameHbgenes. Blood hemoglobin proteins are encoded by a large family ofhemoglobin(Hb) gene family members, which demonstrate coordinated expression patterns, subject to various organismal (e.g., period of life history) and environmental influences (e.g., oxygen availability). Surprisingly, we found that geographically distinct populations showed mostly divergent patterns ofHbgene expression. Cavefish from two cave localities, Pachón and Tinaja, have a more recent shared origin, and show more similarHbexpression patterns as adults. However, during embryonic phases, Pachón and Tinaja show significant variability in timing of peak expression ofHbfamily members. In sum, the transcriptomic underpinnings ofHbgene expression represents a complex composite of shared and divergent expression patterns across three captive cavefish populations. We conclude that these differential patterns are likely influenced by life history, and the unique cave conditions in which these animals evolved.
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SAXS structure of homodimeric oxyHemoglobin III from bivalve Lucina pectinata
Abstract Hemoglobin III (HbIII) is one of the two oxygen reactive hemoproteins present in the bivalve,Lucina pectinata. The clam inhabits a sulfur‐rich environment and HbIII is the only hemoprotein present in the system which does not yet have a structure described elsewhere. It is known that HbIII exists as a heterodimer with hemoglobin II (HbII) to generate the stable Oxy(HbII‐HbIII) complex but it remains unknown if HbIII can form a homodimeric species. Here, a new chromatographic methodology to separate OxyHbIII from the HbII‐HbIII dimer has been developed, employing a fast performance liquid chromatography and ionic exchange chromatography column. The nature of OxyHbIII in solution at concentrations from 1.6 mg/mL to 20.4 mg/mL was studied using small angle X‐ray scattering (SAXS). The results show that at all concentrations, the Oxy(HbIII‐HbIII) dimer dominates in solution. However, as the concentration increases to nonphysiological values, 20.4 mg/mL, HbIII forms a 30% tetrameric fraction. Thus, there is a direct relationship between the Oxy(HbIII‐HbIII) oligomeric form and hemoglobin concentration. We suggest it is likely that the OxyHbIII dimer contributes to active oxygen transport in tissues ofL pectinata, where the Oxy(HbII‐HbIII) complex is not present.
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- Award ID(s):
- 1231306
- PAR ID:
- 10587702
- Publisher / Repository:
- Biopolymers
- Date Published:
- Journal Name:
- Biopolymers
- Volume:
- 112
- Issue:
- 6
- ISSN:
- 0006-3525
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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- Free Publicly Accessible Full Text
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Accepted Manuscript
- Journal Article:
- https://doi.org/10.1002/bip.23427
