0000000001295772
AUTHOR
Christian Pick
showing 11 related works from this author
Additional file 1 of Diversity, evolution, and function of myriapod hemocyanins
2018
Table S1. List of primer sequences used in this study. (PDF 64 kb)
The diversity and evolution of chelicerate hemocyanins
2012
Abstract Background Oxygen transport in the hemolymph of many arthropod species is facilitated by large copper-proteins referred to as hemocyanins. Arthropod hemocyanins are hexamers or oligomers of hexamers, which are characterized by a high O2 transport capacity and a high cooperativity, thereby enhancing O2 supply. Hemocyanin subunit sequences had been available from horseshoe crabs (Xiphosura) and various spiders (Araneae), but not from any other chelicerate taxon. To trace the evolution of hemocyanins and the emergence of the large hemocyanin oligomers, hemocyanin cDNA sequences were obtained from representatives of selected chelicerate classes. Results Hemocyanin subunits from a sea s…
Structure, diversity and evolution of myriapod hemocyanins
2014
Oxygen transport in the hemolymph of many arthropods is mediated by hemocyanins, large copper-containing proteins that are well-studied in Chelicerata and Crustacea, but had long been considered unnecessary in the subphylum of Myriapoda. Only recently has it become evident that hemocyanins are present in Scutigeromorpha (Chilopoda) and Spirostreptida (Diplopoda). Here we present evidence for a more widespread occurrence of hemocyanin in the myriapods. By means of RT-PCR, western blotting and database searches, hemocyanins were identified in the symphylans Hanseniella audax and Symphylella vulgaris, the chilopod Scolopendra subspinipes dehaani and the diplopod Polydesmus angustus. No hemocya…
Diversity of stonefly hexamerins and implication for the evolution of insect storage proteins
2007
Hexamerins are large storage proteins of insects in the 500 kDa range that evolved from the copper-containing hemocyanins. Hexamerins have been found at high concentration in the hemolymph of many insect taxa, but have remained unstudied in relatively basal taxa. To obtain more detailed insight about early hexamerin evolution, we have studied hexamerins in stoneflies (Plecoptera). Stoneflies are also the only insects for which a functional hemocyanin is known to co-occur with hexamerins in the hemolymph. Here, we identified hexamerins in five plecopteran species and obtained partial cDNA sequences from Perla marginata (Perlidae), Nemoura sp. (Nemouridae), Taeniopteryx burksi (Taeniopterygid…
Molecular characterization of hemocyanin and hexamerin from the firebrat Thermobia domestica (Zygentoma).
2008
Hexapods possess a tracheal system that enables the transport of oxygen to the inner organs. Although respiratory proteins have been considered unnecessary in most Hexapoda for this reason, we recently showed the presence of a functional hemocyanin in the stonefly Perla marginata. Here we report the identification and molecular characterization of a hemocyanin from Zygentoma (Thysanura). We obtained the full length cDNA of two distinct subunit types from the firebrat Thermobia domestica, and partial sequences of the orthologs from the silverfish Lepisma saccharina. The native T. domestica hemocyanin subunits both consist of 658 amino acids, but a signal peptide for transmembrane transport i…
Diversity, evolution, and function of myriapod hemocyanins.
2018
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-…
Additional file 6: of Diversity, evolution, and function of myriapod hemocyanins
2018
Table S3. Expression of hemocyanin subunit mRNA in myriapods. (PDF 72 kb)
Additional file 2 of Diversity, evolution, and function of myriapod hemocyanins
2018
Table S2. List of sequences used in this study. (DOCX 24 kb)
Additional file 3: of Diversity, evolution, and function of myriapod hemocyanins
2018
Figure S1. Multiple sequence alignment of myriapod hemocyanins and phenoloxidases in FASTA format. (PDF 101 kb)
Additional file 4: of Diversity, evolution, and function of myriapod hemocyanins
2018
Data S1. Nucleotide sequences of the Hc and PPO cDNAs and gene identified in this study. (ZIP 81 kb)
Additional file 5: of Diversity, evolution, and function of myriapod hemocyanins
2018
Figure S2. The mRNA levels of Hc subunits were determined by RNA-Seq based on the transcriptomes (Table 1) and displayed as log RPKM values. (TIF 3 mb)