dc.creator | Villalobo Polo, Eduardo | es |
dc.creator | Moch, Clara | es |
dc.creator | Fryd Versavel, Ghislaine | es |
dc.creator | Fleury Aubusson, Anne | es |
dc.creator | Morin, Loïc | es |
dc.date.accessioned | 2017-07-13T14:33:41Z | |
dc.date.available | 2017-07-13T14:33:41Z | |
dc.date.issued | 2003-12 | |
dc.identifier.citation | Villalobo Polo, E., Moch, C., Fryd Versavel, G., Fleury Aubusson, A. y Morin, L. (2003). Cysteine Proteases and Cell Differentiation: Excystment of the Ciliated Protist Sterkiella histriomuscorum. Eukaryotic Cell, 2 (6), 1234-1245. | |
dc.identifier.issn | 1535-9778 (impreso) | es |
dc.identifier.issn | 1535-9786 (electronico) | es |
dc.identifier.uri | http://hdl.handle.net/11441/62486 | |
dc.description.abstract | The process of excystment of Sterkiella histriomuscorum (Ciliophora, Oxytrichidae) leads in a few hours, through a massive influx of water and the resorption of the cyst wall, from an undifferentiated resting cyst to a highly differentiated and dividing vegetative cell. While studying the nature of the genes involved in this process, we isolated three different cysteine proteases genes, namely, a cathepsin B gene, a cathepsin L-like gene, and a calpain-like gene. Excystation was selectively inhibited at a precise differentiating stage by cysteine proteases inhibitors, suggesting that these proteins are specifically required during the excystment process. Reverse transcription-PCR experiments showed that both genes display differential expression between the cyst and the vegetative cells. A phylogenetic analysis showed for the first time that the cathepsin B tree is paraphyletic and that the diverging S. histriomuscorum cathepsin B is closely related to its Giardia homologues, which take part in the cyst wall breakdown process. The deduced cathepsin L-like protein sequence displays the structural signatures and phylogenetic relationships of cathepsin H, a protein that is known only in plants and animals and that is involved in the degradation of extracellular matrix components in cancer diseases. The deduced calpain-like protein sequence does not display the calcium-binding domain of conventional calpains; it belongs to a diverging phylogenetic cluster that includes Aspergillus palB, a protein which is involved in a signal transduction pathway that is sensitive to ambient pH. | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | American Society for Microbiology | es |
dc.relation.ispartof | Eukaryotic Cell, 2 (6), 1234-1245. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | Cysteine Proteases and Cell Differentiation: Excystment of the Ciliated Protist Sterkiella histriomuscorum | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Microbiología | es |
dc.relation.publisherversion | http://dx.doi.org/10.1128/EC.2.6.1234–1245.2003 | es |
dc.identifier.doi | 10.1128/EC.2.6.1234–1245.2003 | es |
idus.format.extent | 12 p. | es |
dc.journaltitle | Eukaryotic Cell | es |
dc.publication.volumen | 2 | es |
dc.publication.issue | 6 | es |
dc.publication.initialPage | 1234 | es |
dc.publication.endPage | 1245 | es |