Wider than Thought Phylogenetic Occurrence of Apicortin, A Characteristic Protein of Apicomplexan Parasites

Orosz, Ferenc

doi:10.1007/s00239-016-9749-5

Cited by 13 publications

(19 citation statements)

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“…The sequence conservation among the TgDCX orthologues is mostly restricted to the predicted P25-alpha and doublecortin domains ( Figure 7A, Table 1) (Orosz, 2009;Orosz, 2016).…”

Section: Comparison Of the Structure Microtubule Association Conoidmentioning

confidence: 99%

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A doublecortin-domain protein of Toxoplasma and its orthologues bind to and modify the structure and organization of tubulin polymers

Leung

Nagayasu

Hwang

et al. 2019

Preprint

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TgDCX is a doublecortin-domain protein associated with the conoid fibers, a set of strongly curved non-tubular tubulin-polymers in Toxoplasma. TgDCX deletion impairs conoid structure and parasite invasion. TgDCX contains two tubulin-binding domains: a partial P25-alpha and the DCX/doublecortin domain. Orthologues are found in apicomplexans and their free-living relatives Chromera and Vitrella. We report that isolated TgDCX-containing conoid fibers retain their pronounced curvature, but loss of TgDCX destabilizes the fibers. We crystallized and determined the 3D-structure of the DCX-domain, which is similar to those of human doublecortin and well-conserved among TgDCX orthologues. However, the orthologues vary widely in targeting to the conoid in Toxoplasma and in modulating microtubule organization in Xenopus cells. Several orthologues bind to microtubules in Xenopus cells, but only TgDCX generates short, strongly curved microtubule arcs. EM analysis shows microtubules decorated with TgDCX bundled into rafts, often bordered on one edge by a "C"-shaped incomplete tube. A Chromera orthologue closely mimics TgDCX targeting in Toxoplasma and binds to microtubules in Xenopus cells, but does not generate arcs or "C"-shaped tubes, and fails to rescue the defects of the TgDCX-knockout parasite. These observations suggest that species-specific features of TgDCX enable it to generate strongly curved tubulin-polymers to support efficient host-cell invasion.

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“…The sequence conservation among the TgDCX orthologues is mostly restricted to the predicted P25-alpha and doublecortin domains ( Figure 7A, Table 1) (Orosz, 2009;Orosz, 2016).…”

Section: Comparison Of the Structure Microtubule Association Conoidmentioning

confidence: 99%

“…Although both the P25α and DCX domains are ubiquitous among metazoa, the presence of both domains in the same molecule appears to be almost exclusively an apicomplexan feature (Orosz, 2009;Orosz, 2016). This combination is found in all sequenced genomes of apicomplexans (e.g.…”

Section: Introductionmentioning

confidence: 99%

A doublecortin-domain protein of Toxoplasma and its orthologues bind to and modify the structure and organization of tubulin polymers

Leung

Nagayasu

Hwang

et al. 2019

Preprint

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“…All sequenced apicomplexan genomes (Nagayasu et al. , 2006; Orosz, 2009), as well as the genomes of chromerids and perkinsids (Orosz, 2016), have orthologues of TgDCX, recognizable by having DCX and P25-α domains together in the same molecule. Outside this group, this domain arrangement is found only in an early-diverging metazoan ( Trichoplax adhaerens , phylum Placozoa; Orosz, 2009).…”

Section: Introductionmentioning

confidence: 99%

Loss of a doublecortin (DCX)-domain protein causes structural defects in a tubulin-based organelle of Toxoplasma gondii and impairs host-cell invasion

Nagayasu

Hwang

et al. 2017

MBoC

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“…Although the kit should be effective in removing ∼90% or more of rRNA (Cui et al, 2010), the raw data from P. elegans contained a considerable proportion of ribosomal gene sequences (71.9% of all reads), indicating rRNA depletion was not effective. Identity of contaminating sequences is only rarely investigated in transcriptome studies (e.g., Orosz, 2016;Zhu, Wang, & Pelosi, 2016), but should be mentioned in the case that not all contaminating sequences are effectively removed. Our data suggest that it is even less effective for non-vertebrate species.…”

Section: Discussionmentioning

confidence: 99%

“…This finding was not unexpected since whole worms were used and, therefore, RNA from other species (gut contents, parasites, pathogens, and associated microbiota) was also likely present. Identity of contaminating sequences is only rarely investigated in transcriptome studies (e.g., Orosz, 2016;Zhu, Wang, & Pelosi, 2016), but should be mentioned in the case that not all contaminating sequences are effectively removed.…”

Section: Discussionmentioning

confidence: 99%

De novo transcriptome assembly and developmental mode specific gene expression of Pygospio elegans

Heikkinen

Kesäniemi

Knott

2017

Evolution and Development

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Species with multiple different larval developmental modes are interesting models for the study of mechanisms underlying developmental mode transitions and life history evolution. Pygospio elegans, a small, tube-dwelling polychaete worm commonly found in estuarine and marine habitats around the northern hemisphere, is one species with variable developmental modes. To provide new genomic resources for studying P. elegans and to address the differences in gene expression between individuals producing offspring with different larval developmental modes, we performed whole transcriptome Illumina RNA sequencing of adult worms from two populations and prepared a de novo assembly of the P. elegans transcriptome. The transcriptome comprises 66,233 unigenes, of which 33,807 contain predicted coding sequences, 26,448 have at least one functional annotation, and 3,076 are classified as putative long non-coding RNAs. We found more than 8,000 unigenes significantly differentially expressed between adult worms from populations producing either planktonic or benthic larvae. This comprehensive transcriptome resource for P. elegans adds to the available genomic data for annelids and can be used to uncover mechanisms allowing developmental variation in this and potentially other marine invertebrate species.

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Wider than Thought Phylogenetic Occurrence of Apicortin, A Characteristic Protein of Apicomplexan Parasites

Cited by 13 publications

References 50 publications

A doublecortin-domain protein of Toxoplasma and its orthologues bind to and modify the structure and organization of tubulin polymers

A doublecortin-domain protein of Toxoplasma and its orthologues bind to and modify the structure and organization of tubulin polymers

Loss of a doublecortin (DCX)-domain protein causes structural defects in a tubulin-based organelle of Toxoplasma gondii and impairs host-cell invasion

De novo transcriptome assembly and developmental mode specific gene expression of Pygospio elegans

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