Diversity, evolution, and function of myriapod hemocyanins
| Autor: | Thorsten Burmester, Nadja Hellmann, Christian Pick, Rosa Fernández, Samantha Scherbaum |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Arthropoda Evolution medicine.medical_treatment Myriapoda Zoology chemical and pharmacologic phenomena complex mixtures Hemocyanin Pauropoda Evolution Molecular 03 medical and health sciences Hemolymph medicine QH359-425 Animals Amino Acid Sequence RNA Messenger Arthropods Ecology Evolution Behavior and Systematics Phylogeny Binding Sites biology Base Sequence Monophenol Monooxygenase Genetic Variation hemic and immune systems biology.organism_classification Respiratory protein Oxygen Protein Subunits 030104 developmental biology Hemocyanins Phenoloxidase Subunit diversity Arthropod Symphyla Centipede Copper Research Article |
| Zdroj: | BMC Evolutionary Biology BMC Evolutionary Biology, Vol 18, Iss 1, Pp 1-13 (2018) |
| ISSN: | 1471-2148 |
| Popis: | Background Hemocyanin transports O2 in the hemolymph of many arthropod species. Such respiratory proteins have long been considered unnecessary in Myriapoda. As a result, the presence of hemocyanin in Myriapoda has long been overlooked. We analyzed transcriptome and genome sequences from all major myriapod taxa – Chilopoda, Diplopoda, Symphyla, and Pauropoda – with the aim of identifying hemocyanin-like proteins. Results We investigated the genomes and transcriptomes of 56 myriapod species and identified 46 novel full-length hemocyanin subunit sequences in 20 species of Chilopoda, Diplopoda, and Symphyla, but not Pauropoda. We found in Cleidogona sp. (Diplopoda, Chordeumatida) a hemocyanin-like sequence with mutated copper-binding centers, which cannot bind O2. An RNA-seq approach showed markedly different hemocyanin mRNA levels from ~ 6 to 25,000 reads per kilobase per million reads. To evaluate the contribution of hemocyanin to O2 transport, we specifically studied the hemocyanin of the centipede Scolopendra dehaani. This species harbors two distinct hemocyanin subunits with low expression levels. We showed cooperative O2 binding in the S. dehaani hemolymph, indicating that hemocyanin supports O2 transport even at low concentration. Further, we demonstrated that hemocyanin is > 1500-fold more highly expressed in the fertilized egg than in the adult. Conclusion Hemocyanin was most likely the respiratory protein in the myriapod stem-lineage, but multiple taxa may have independently lost hemocyanin and thus the ability of efficient O2 transport. In myriapods, hemocyanin is much more widespread than initially appreciated. Some myriapods express hemocyanin only at low levels, which are, nevertheless, sufficient for O2 supply. Notably, also in myriapods, a non-respiratory protein similar to insect storage hexamerins evolved from the hemocyanin. Electronic supplementary material The online version of this article (10.1186/s12862-018-1221-2) contains supplementary material, which is available to authorized users. |
| Databáze: | OpenAIRE |
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