The Expression of Tubulin and Tektin Genes in Dicyemid Mesozoans (Phylum: Dicyemida)

Ogino, Kazutoyo; Tsuneki, Kazuhiko; Furuya, Hidetaka

doi:10.1645/ge-1037r.1

Cited by 5 publications

(4 citation statements)

References 59 publications

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“…These data sets contain 17,044 introns and 16,295 independent splice sequences derived from several model organisms, including animals, plants, and fungi. The dicyemid introns showed similar frequency in the phase distribution, i.e., 13 (54%), 5 (21%), and 6 (25%) in the total 24 introns in tubulin (alpha, beta), tektin (B, C), and Dicyema-clp1 (Ogino et al, 2007;the present study). As far as the number and the frequency distribution of intron phases are concerned, the Dicyema-clp1 possesses the usual introns.…”

Section: Discussionsupporting

confidence: 70%

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Cloning of Chitinase-Like Protein1 Cdna From Dicyemid Mesozoans (Phylum: Dicyemida)

Ogino¹,

Tsuneki²,

Furuya³

2007

Journal of Parasitology

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Dicyemid mesozoans are endoparasites found in the renal sacs of benthic cephalopods. Adult dicyemids insert the distinct anterior region, termed a "calotte," into renal tubules of the host. We cloned cDNA encoding chitinase-like protein from the dicyemid Dicyema japonicum (Dicyema-clp 1), and also cloned the gene fragment corresponding to the cDNA. Dicyema-clp1 has the hydrophobic amino acid-rich region, but not the chitin-binding domains at the C terminus. Analyses using the SignalP prediction program suggest this hydrophobic amino acid-rich region is the anchor sequence to plasma membranes. The putative catalytic site in glyco18 domain exhibited 1 substitution from aspartic acid to asparagine. The gene fragment had short 9 introns (22-26 bp), and the coding sequence consisted of 10 exons (30-233 bp). Specific and strong expression of Dicyema-clpl was detected in the calotte of vermiform stages by whole mount in situ hybridization. N-acetyl-D-glucosamine was detected on the outer surface of both peripheral cells of dicyemids and epidermal cells of host renal appendages. Dicyema-clp appears to be associated with N-acetyl-D-glucosamine in the interface between dicyemid peripheral cells and epidermal cells of the host renal appendage, and possibly aids in adhering the calotte to host epidermal cells.

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Section: Discussionsupporting

confidence: 70%

“…The accelerated molecular evolution may be attributed to the fact that dicyemids are small endoparasites and have a short generation time. Ogino et al (2007) reported short lengths of introns in tubulin and tektin genes in dicyemids. Aruga et al (pers.…”

Section: Discussionmentioning

confidence: 99%

Cloning of Chitinase-Like Protein1 Cdna From Dicyemid Mesozoans (Phylum: Dicyemida)

Ogino¹,

Tsuneki²,

Furuya³

2007

Journal of Parasitology

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“…T7 or SP6 RNA polymerase (Roche) was used in the in vitro transcription to synthesize an antisense RNA probe, and a sense RNA probe was used as a negative control for hybridization. Whole-mount in situ hybridization was conducted by previously described methods (Ogino et al, 2007a(Ogino et al, , 2007b.…”

Section: Whole-mount In Situ Hybridizationmentioning

confidence: 99%

Phylogenetic Analysis of Dicyemid Mesozoans (Phylum Dicyemida) From Innexin Amino Acid Sequences: Dicyemids Are Not Related to Platyhelminthes

Suzuki

Ogino

Tsuneki

et al. 2010

Journal of Parasitology

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Dicyemid mesozoans are endoparasites, or endosymbionts, found only in the renal sac of benthic cephalopod molluscs. The body organization of dicyemids is very simple, consisting of usually 10 to 40 cells, with neither body cavities nor differentiated organs. Dicyemids were considered as primitive animals, and the out-group of all metazoans, or as occupying a basal position of lophotrochozoans close to flatworms. We cloned cDNAs encoding for the gap junction component proteins, innexin, from the dicyemids. Its expression pattern was observed by whole-mount in situ hybridization. In adult individuals, the innexin was expressed in calottes, infusorigens, and infusoriform embryos. The unique temporal pattern was observed in the developing infusoriform embryos. Innexin amino acid sequences had taxon-specific indels which enabled identification of the 3 major protostome lineages, i.e., 2 ecdysozoans (arthropods and nematodes) and the lophotrochozoans. The dicyemids show typical, lophotrochozoan-type indels. In addition, the Bayesian and maximum likelihood trees based on the innexin amino acid sequences suggested dicyemids to be more closely related to the higher lophotrochozoans than to the flatworms. Flatworms were the sister group, or consistently basal, to the other lophotrochozoan clade that included dicyemids, annelids, molluscs, and brachiopods.

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“…After many years of being regarded as an obscure group of specialized proteins, they have become important, as related genes are found in every newly sequenced eukaryotic genome. Tektins will increasingly be used in phylogenetic studies [ 21 - 23 , 30 ] and may turn out to vary even among human beings and be useful, for example, in tracking population movements.…”

Section: Frontiersmentioning

confidence: 99%

The tektin family of microtubule-stabilizing proteins

Amos

2008

Genome Biol

107

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Protein family reviewT Th he e t te ek kt ti in n f fa am mi il ly y o of f m mi ic cr ro ot tu ub bu ul le e--s st ta ab bi il li iz zi in ng g p pr ro ot te ei in ns s Linda A Amos Address: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK. Email: laa@mrc-lmb.cam.ac.uk S Su um mm ma ar ry yTektins are insoluble α-helical proteins essential for the construction of cilia and flagella and are found throughout the eukaryotes apart from higher plants. Being almost universal but still fairly free to mutate, their coding sequences have proved useful for estimating the evolutionary relationships between closely related species. Their protein molecular structure, typically consisting of four coiled-coil rod segments connected by linkers, resembles that of intermediate filament (IF) proteins and lamins. Tektins assemble into continuous rods 2 nm in diameter that are probably equivalent to subfilaments of the 10 nm diameter IFs. Tektin and IF rod sequences both have a repeating pattern of charged amino acids superimposed on the seven-amino-acid hydrophobic pattern of coiled-coil proteins. The length of the repeat segment matches that of tubulin subunits, suggesting that tektins and tubulins may have coevolved, and that lamins and IFs may have emerged later as modified forms of tektin. Unlike IFs, tektin sequences include one copy of a conserved peptide of nine amino acids that may bind tubulin. The 2 nm filaments associate closely with tubulin in doublet and triplet microtubules of axonemes and centrioles, respectively, and help to stabilize these structures. Their supply restricts the assembled lengths of cilia and flagella. In doublet microtubules, the 2 nm filaments may also help to organize the longitudinal spacing of accessory structures, such as groups of inner dynein arms and radial spokes. The electronic version of this article is the complete one and can be found online at

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The Expression of Tubulin and Tektin Genes in Dicyemid Mesozoans (Phylum: Dicyemida)

Cited by 5 publications

References 59 publications

Cloning of Chitinase-Like Protein1 Cdna From Dicyemid Mesozoans (Phylum: Dicyemida)

Cloning of Chitinase-Like Protein1 Cdna From Dicyemid Mesozoans (Phylum: Dicyemida)

Phylogenetic Analysis of Dicyemid Mesozoans (Phylum Dicyemida) From Innexin Amino Acid Sequences: Dicyemids Are Not Related to Platyhelminthes

The tektin family of microtubule-stabilizing proteins

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