Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species
Parvalbumins are small molecules with important functions in Ca<sup>2+</sup> signaling, but their sequence comparisons to date, especially in fish, have been relatively poor. We here, characterize sequence motifs that distinguish parvalbumin subfamilies across vertebrate species, as well...
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MDPI AG
2022-11-01
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| Online Access: | https://www.mdpi.com/2079-7737/11/12/1713 |
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| author | Johannes M. Dijkstra Yasuto Kondo |
| author_facet | Johannes M. Dijkstra Yasuto Kondo |
| author_sort | Johannes M. Dijkstra |
| collection | DOAJ |
| description | Parvalbumins are small molecules with important functions in Ca<sup>2+</sup> signaling, but their sequence comparisons to date, especially in fish, have been relatively poor. We here, characterize sequence motifs that distinguish parvalbumin subfamilies across vertebrate species, as well as those that distinguish individual parvalbumins (orthologues) in fish, and map them to known parvalbumin structures. As already observed by others, all classes of jawed vertebrates possess parvalbumins of both the α-parvalbumin and oncomodulin subfamilies. However, we could not find convincing phylogenetic support for the common habit of classifying all non-α-parvalbumins together as “β-parvalbumins.” In teleost (modern bony) fish, we here distinguish parvalbumins 1-to-10, of which the gene copy number can differ between species. The genes for α-parvalbumins (<i>pvalb6</i> and <i>pvalb7</i>) and oncomodulins (<i>pvalb8</i> and <i>pvalb9</i>) are well conserved between teleost species, but considerable variation is observed in their copy numbers of the non-α/non-oncomodulin genes <i>pvalb1-to-5</i> and <i>pvalb10</i>. Teleost parvalbumins 1-to-4 are hardly distinguishable from each other and are highly expressed in muscle, and described allergens belong to this subfamily. However, in some fish species α-parvalbumin expression is also high in muscle. Pvalb5 and pvalb10 molecules form distinct lineages, the latter even predating the origin of teleosts, but have been lost in some teleost species. The present study aspires to be a frame of reference for future studies trying to compare different parvalbumins. |
| first_indexed | 2024-03-09T17:18:51Z |
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| language | English |
| last_indexed | 2024-03-09T17:18:51Z |
| publishDate | 2022-11-01 |
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| spelling | doaj.art-0ee6e7c57f2c4589923ae7a534df13752023-11-24T13:22:05ZengMDPI AGBiology2079-77372022-11-011112171310.3390/biology11121713Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod SpeciesJohannes M. Dijkstra0Yasuto Kondo1Center for Medical Science, Fujita Health University, Dengaku-gakubo 1-98, Toyoake 470-1192, JapanDepartment of Pediatrics, Fujita Health University Bantane Hospital, Otobashi 3-6-10, Nakagawa, Nagoya 454-8509, JapanParvalbumins are small molecules with important functions in Ca<sup>2+</sup> signaling, but their sequence comparisons to date, especially in fish, have been relatively poor. We here, characterize sequence motifs that distinguish parvalbumin subfamilies across vertebrate species, as well as those that distinguish individual parvalbumins (orthologues) in fish, and map them to known parvalbumin structures. As already observed by others, all classes of jawed vertebrates possess parvalbumins of both the α-parvalbumin and oncomodulin subfamilies. However, we could not find convincing phylogenetic support for the common habit of classifying all non-α-parvalbumins together as “β-parvalbumins.” In teleost (modern bony) fish, we here distinguish parvalbumins 1-to-10, of which the gene copy number can differ between species. The genes for α-parvalbumins (<i>pvalb6</i> and <i>pvalb7</i>) and oncomodulins (<i>pvalb8</i> and <i>pvalb9</i>) are well conserved between teleost species, but considerable variation is observed in their copy numbers of the non-α/non-oncomodulin genes <i>pvalb1-to-5</i> and <i>pvalb10</i>. Teleost parvalbumins 1-to-4 are hardly distinguishable from each other and are highly expressed in muscle, and described allergens belong to this subfamily. However, in some fish species α-parvalbumin expression is also high in muscle. Pvalb5 and pvalb10 molecules form distinct lineages, the latter even predating the origin of teleosts, but have been lost in some teleost species. The present study aspires to be a frame of reference for future studies trying to compare different parvalbumins.https://www.mdpi.com/2079-7737/11/12/1713parvalbuminoncomodulinfishevolutionsequencestructure |
| spellingShingle | Johannes M. Dijkstra Yasuto Kondo Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species Biology parvalbumin oncomodulin fish evolution sequence structure |
| title | Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species |
| title_full | Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species |
| title_fullStr | Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species |
| title_full_unstemmed | Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species |
| title_short | Comprehensive Sequence Analysis of Parvalbumins in Fish and Their Comparison with Parvalbumins in Tetrapod Species |
| title_sort | comprehensive sequence analysis of parvalbumins in fish and their comparison with parvalbumins in tetrapod species |
| topic | parvalbumin oncomodulin fish evolution sequence structure |
| url | https://www.mdpi.com/2079-7737/11/12/1713 |
| work_keys_str_mv | AT johannesmdijkstra comprehensivesequenceanalysisofparvalbuminsinfishandtheircomparisonwithparvalbuminsintetrapodspecies AT yasutokondo comprehensivesequenceanalysisofparvalbuminsinfishandtheircomparisonwithparvalbuminsintetrapodspecies |