Bioinformatic Characterization and Molecular Evolution of the <i>Lucina pectinata</i> Hemoglobins
(1) Introduction: <i>Lucina pectinata</i> is a clam found in sulfide-rich mud environments that has three hemoglobins believed to be responsible for the transport of hydrogen sulfide (HbI<sub>Lp</sub>) and oxygen (HbII<sub>Lp</sub> and HbIII<sub>Lp</sub&g...
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MDPI AG
2022-11-01
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| Series: | Genes |
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| Online Access: | https://www.mdpi.com/2073-4425/13/11/2041 |
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| author | Ingrid M. Montes-Rodríguez Carmen L. Cadilla Juan López-Garriga Ricardo González-Méndez |
| author_facet | Ingrid M. Montes-Rodríguez Carmen L. Cadilla Juan López-Garriga Ricardo González-Méndez |
| author_sort | Ingrid M. Montes-Rodríguez |
| collection | DOAJ |
| description | (1) Introduction: <i>Lucina pectinata</i> is a clam found in sulfide-rich mud environments that has three hemoglobins believed to be responsible for the transport of hydrogen sulfide (HbI<sub>Lp</sub>) and oxygen (HbII<sub>Lp</sub> and HbIII<sub>Lp</sub>) to chemoautotrophic endosymbionts. The physiological roles and evolution of these globins in sulfide-rich environments are not well understood. (2) Methods: We performed bioinformatic and phylogenetic analyses with 32 homologous mollusk globin sequences. Phylogenetics suggests a first gene duplication resulting in sulfide binding and oxygen binding genes. A more recent gene duplication gave rise to the two oxygen-binding hemoglobins. Multidimensional scaling analysis of the sequence space shows evolutionary drift of HbII<sub>Lp</sub> and HbIII<sub>Lp</sub>, while HbI<sub>Lp</sub> was closer to the <i>Calyptogena</i> hemoglobins. Further corroboration is seen by conservation in the coding region of hemoglobins from <i>L. pectinata</i> compared to those from <i>Calyptogena</i>. (3) Conclusions: Presence of glutamine in position E7 in organisms living in sulfide-rich environments can be considered an adaptation to prevent loss of protein function. In HbI<sub>Lp</sub> a substitution of phenylalanine in position B10 is accountable for its unique reactivity towards H<sub>2</sub>S. It appears that HbI<sub>Lp</sub> has been changing over time, apparently not subject to functional constraints of binding oxygen, and acquired a unique function for a specialized environment. |
| first_indexed | 2024-03-09T19:03:51Z |
| format | Article |
| id | doaj.art-bc5632efd90249de8ed552945c4f3fa8 |
| institution | Directory Open Access Journal |
| issn | 2073-4425 |
| language | English |
| last_indexed | 2024-03-09T19:03:51Z |
| publishDate | 2022-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Genes |
| spelling | doaj.art-bc5632efd90249de8ed552945c4f3fa82023-11-24T04:48:51ZengMDPI AGGenes2073-44252022-11-011311204110.3390/genes13112041Bioinformatic Characterization and Molecular Evolution of the <i>Lucina pectinata</i> HemoglobinsIngrid M. Montes-Rodríguez0Carmen L. Cadilla1Juan López-Garriga2Ricardo González-Méndez3Cancer Biology Division, PROMIC, Comprehensive Cancer Center of the University of Puerto Rico, San Juan, PR 00936-3027, USADepartment of Biochemistry, School of Medicine, University of Puerto Rico-Medical Sciences Campus, San Juan, PR 00936-5067, USADepartment of Chemistry, Faculty of Arts and Sciences, University of Puerto Rico—Mayagüez Campus, Mayagüez, PR 00681-9000, USADepartment of Radiological Sciences, School of Medicine, University of Puerto Rico-Medical Sciences Campus, San Juan, PR 00936-5067, USA(1) Introduction: <i>Lucina pectinata</i> is a clam found in sulfide-rich mud environments that has three hemoglobins believed to be responsible for the transport of hydrogen sulfide (HbI<sub>Lp</sub>) and oxygen (HbII<sub>Lp</sub> and HbIII<sub>Lp</sub>) to chemoautotrophic endosymbionts. The physiological roles and evolution of these globins in sulfide-rich environments are not well understood. (2) Methods: We performed bioinformatic and phylogenetic analyses with 32 homologous mollusk globin sequences. Phylogenetics suggests a first gene duplication resulting in sulfide binding and oxygen binding genes. A more recent gene duplication gave rise to the two oxygen-binding hemoglobins. Multidimensional scaling analysis of the sequence space shows evolutionary drift of HbII<sub>Lp</sub> and HbIII<sub>Lp</sub>, while HbI<sub>Lp</sub> was closer to the <i>Calyptogena</i> hemoglobins. Further corroboration is seen by conservation in the coding region of hemoglobins from <i>L. pectinata</i> compared to those from <i>Calyptogena</i>. (3) Conclusions: Presence of glutamine in position E7 in organisms living in sulfide-rich environments can be considered an adaptation to prevent loss of protein function. In HbI<sub>Lp</sub> a substitution of phenylalanine in position B10 is accountable for its unique reactivity towards H<sub>2</sub>S. It appears that HbI<sub>Lp</sub> has been changing over time, apparently not subject to functional constraints of binding oxygen, and acquired a unique function for a specialized environment.https://www.mdpi.com/2073-4425/13/11/2041<i>Lucina pectinata</i><i>L. pectinate</i>hemoglobinssulphur-binding hemoglobinsbioinformaticsphylogenetics of hemoglobins in mollusks |
| spellingShingle | Ingrid M. Montes-Rodríguez Carmen L. Cadilla Juan López-Garriga Ricardo González-Méndez Bioinformatic Characterization and Molecular Evolution of the <i>Lucina pectinata</i> Hemoglobins Genes <i>Lucina pectinata</i> <i>L. pectinate</i> hemoglobins sulphur-binding hemoglobins bioinformatics phylogenetics of hemoglobins in mollusks |
| title | Bioinformatic Characterization and Molecular Evolution of the <i>Lucina pectinata</i> Hemoglobins |
| title_full | Bioinformatic Characterization and Molecular Evolution of the <i>Lucina pectinata</i> Hemoglobins |
| title_fullStr | Bioinformatic Characterization and Molecular Evolution of the <i>Lucina pectinata</i> Hemoglobins |
| title_full_unstemmed | Bioinformatic Characterization and Molecular Evolution of the <i>Lucina pectinata</i> Hemoglobins |
| title_short | Bioinformatic Characterization and Molecular Evolution of the <i>Lucina pectinata</i> Hemoglobins |
| title_sort | bioinformatic characterization and molecular evolution of the i lucina pectinata i hemoglobins |
| topic | <i>Lucina pectinata</i> <i>L. pectinate</i> hemoglobins sulphur-binding hemoglobins bioinformatics phylogenetics of hemoglobins in mollusks |
| url | https://www.mdpi.com/2073-4425/13/11/2041 |
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