Myriapod haemocyanin: the first three-dimensional reconstruction of Scolopendra subspinipes and preliminary structural analysis of S. viridicornis
Open Access
- 1 April 2020
- journal article
- research article
- Published by The Royal Society in Open Biology
- Vol. 10 (4), 190258
- https://doi.org/10.1098/rsob.190258
Abstract
Haemocyanins (Hcs) are copper-containing, respiratory proteins that occur in the haemolymph of many arthropod species. Here, we report the presence of Hcs in the chilopode Myriapoda, demonstrating that these proteins are more widespread among the Arthropoda than previously thought. The analysis of transcriptome of S. subspinipes subpinipes reveals the presence of two distinct subunits of Hc, where the signal peptide is present, and six of prophenoloxidase (PPO), where the signal peptide is absent, in the 75 kDa range. Size exclusion chromatography profiles indicate different quaternary organization for Hc of both species, which was corroborated by TEM analysis: S. viridicornis Hc is a 6 x 6-mer and S. subspinipes Hc is a 3 x 6-mer, which resembles the half-structure of the 6 x 6-mer but also includes the presence of phenoloxidases, since the 1 x 6-mer quaternary organization is commonly associated with hexamers of PPO. Studies with Chelicerata showed that PPO activity are exclusively associated with the Hcs. This study indicates that Scolopendra may have different proteins playing oxygen transport (Hc) and PO function, both following the hexameric oligomerization observed in Hcs.This publication has 102 references indexed in Scilit:
- Fiji: an open-source platform for biological-image analysisNature Methods, 2012
- Full-length transcriptome assembly from RNA-Seq data without a reference genomeNature Biotechnology, 2011
- Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymesProceedings of the National Academy of Sciences of the United States of America, 2009
- FRODOCK: a new approach for fast rotational protein–protein dockingBioinformatics, 2009
- Structural Mechanism of SDS-Induced Enzyme Activity of Scorpion Hemocyanin Revealed by Electron CryomicroscopyStructure, 2009
- Jalview Version 2—a multiple sequence alignment editor and analysis workbenchBioinformatics, 2009
- Clustal W and Clustal X version 2.0Bioinformatics, 2007
- ProtTest: selection of best-fit models of protein evolutionBioinformatics, 2005
- Crystal structure of a plant catechol oxidase containing a dicopper centerNature Structural & Molecular Biology, 1998
- Multicopper Oxidases and OxygenasesChemical Reviews, 1996