Nucleotide and Deduced Amino Acid Sequences of<i>Biomphalaria glabrata</i>Actin cDNA

Lardans, Vinca; Ringaut, Virginie; Duclermortier, Pascal; Cadoret, Jean‐Paul; Dissous, Colette

doi:10.3109/10425179709034055

Cited by 10 publications

(6 citation statements)

References 15 publications

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“…Actin sequences have been reported and cloned from Echinodermata [26,27], Nematoda [28], insects [29] and crustaceans [30]. Among mollusks, actin sequences from three gastropods have been published [17,31,32]. In bivalves, a partial actin sequence of the oyster C. virginica [20] and the complete sequence of the scallop P. magellanicus [24] and the zebra mussel Dreissena polymorpha [33] are now available.…”

Section: Resultsmentioning

confidence: 99%

“…Encoded by a multigenic family, it displays a very high degree of conservation between species. The promoter for the actin gene has been chosen in several cases since the gene is very abundant and constitutively expressed [14–17]. The identification and isolation of an actin encoding gene in the oyster C. gigas will allow for comparative analysis in functional studies with other genes, studies on population variation and its use in transgenesis [12,18,19].…”

Section: Introductionmentioning

confidence: 99%

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Transient expression assays with the proximal promoter of a newly characterized actin gene from the oyster Crassostrea gigas

et al. 1999

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We undertook the characterization of an actin gene and its proximal promoter in the oyster Crassostrea gigas. A complete actin cDNA was identified, sequenced and its amino acid sequence deduced. Comparative analysis showed a high homology with actin of other species and that this gene is closer to the cytoplasmic form of actins than to the muscle type. A probe derived from the 5P P-untranslated region of the cDNA was then used to isolate the actin gene from a genomic library. The gene was sequenced and shown to contain a single 643 bp intron. A 1670 bp fragment upstream from the open reading frame was isolated and sequenced. This upstream region displays typical features of actins such as a serum response element (CarG box). This fragment was cloned into the promoterless vector pGL3-basic and the resulting construct was transfected into cells of dissociated oyster heart primary cultures. Its capacity to express the luciferase in this in vitro homologous system was monitored and showed high expression levels. This is the first complete actin sequence reported so far for the oyster C. gigas and its promoter is the first available among bivalves.z 1999 Federation of European Biochemical Societies.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Transient expression assays with the proximal promoter of a newly characterized actin gene from the oyster Crassostrea gigas

et al. 1999

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“…The full-length cDNA probe was 32 P-labeled by the Random Primers DNA Labelling System (Invitrogen). A probe corresponding to the complete coding sequence of B. glabrata actin (Lardans et al 1997) was labeled in the same way and used as a control. Hybridization was carried out as described elsewhere (Sambrook & Russell 2001), and blots were exposed overnight to X-Omat AR film (Kodak).…”

Section: Northern and Southern Blottingmentioning

confidence: 99%

A conserved retinoid X receptor (RXR) from the mollusk Biomphalaria glabrata transactivates transcription in the presence of retinoids

Bouton¹,

Escrivà²,

Mendonça³

et al. 2005

Journal of Molecular Endocrinology

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Retinoid X receptors (RXR) are members of the nuclear receptor superfamily of ligand-activated transcription factors that have been characterized in a wide variety of metazoan phyla. They act as heterodimer partners of other nuclear receptors, and in vertebrates also activate transcription as homodimers in the presence of a ligand, 9-cis retinoic acid. In order to test the hypothesis that retinoic acid signaling pathways involving RXRs are present in the Lophotrochozoa, we have sought to isolate conserved members of this family from the platyhelminth parasite Schistosoma mansoni and its intermediate host, the mollusk Biomphalaria glabrata. Here we report that an RXR ortholog from B. glabrata (BgRXR) is better conserved, compared with mouse RXR , both in the DNA-binding domain (89% identity) and in the ligand-binding domain (LBD) (81% identity), than are arthropod homologs. In EMSA, BgRXR binds to the direct repeat response element DR1 as a homodimer or as a heterodimer with mammalian RAR , LXR, FXR or PPAR . When transfected alone into mammalian cell lines, BgRXR transactivated transcription of a reporter gene from the Apo-A1 promoter in the presence of 9-cis retinoic acid or DHA. Constructs with the Gal4 DNA binding domain fused to the hinge and LBDs of BgRXR were used to show that ligand-dependent activation of transcription by BgRXR required its intact AF-2 activation domain, and that the LBD can form homodimers. Finally, the binding of 9-cis retinoic acid preferentially protected the LBD of BgRXR from degradation by trypsin in a proteolysis protection assay. Our results show that BgRXR binds and is activated by retinoids and suggest that retinoid signaling pathways are conserved in the Lophotrochozoa. The nucleotide sequence reported in this paper has been submitted to the GenBank/EBI Data Bank with accession no. AY048663.

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“…A number of B. glabrata genes have been sequenced: actin (Lardans et al, 1997), myoglobin (Dewilde et al, 1998), 18S rDNA (Hanelt et al, 1997, and heat shock protein 70 , and of several factors that may function in defense contexts: signal transduction factor RACK , integrin that functions in the adherence of hemocyte Yoshino, 1998, Davids et al, 1999) and lectins such as selectin (Duclermortier et al, 1999) and FREPs (Adema et al, 1997b). A number of B. glabrata genes have been sequenced: actin (Lardans et al, 1997), myoglobin (Dewilde et al, 1998), 18S rDNA (Hanelt et al, 1997, and heat shock protein 70 , and of several factors that may function in defense contexts: signal transduction factor RACK , integrin that functions in the adherence of hemocyte Yoshino, 1998, Davids et al, 1999) and lectins such as selectin (Duclermortier et al, 1999) and FREPs (Adema et al, 1997b).…”

Section: New Developmentsmentioning

confidence: 99%

Echinostomes as Experimental Models for Biological Research

Fried¹,

Graczyk²

2000

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Nucleotide and Deduced Amino Acid Sequences ofBiomphalaria glabrataActin cDNA

Cited by 10 publications

References 15 publications

Transient expression assays with the proximal promoter of a newly characterized actin gene from the oyster Crassostrea gigas

Transient expression assays with the proximal promoter of a newly characterized actin gene from the oyster Crassostrea gigas

A conserved retinoid X receptor (RXR) from the mollusk Biomphalaria glabrata transactivates transcription in the presence of retinoids

Echinostomes as Experimental Models for Biological Research

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