Cysteine Proteases and Cell Differentiation: Excystment of the Ciliated Protist Sterkiella histriomuscorum
| Autor: | Loïc Morin, Ghislaine Fryd-Versavel, Eduardo Villalobo, Anne Fleury-Aubusson, Clara Moch |
|---|---|
| Přispěvatelé: | Universidad de Sevilla. Departamento de Microbiología |
| Rok vydání: | 2003 |
| Předmět: |
Proteases
Time Factors Leupeptins Genes Protozoan Molecular Sequence Data Protozoan Proteins Cysteine Proteinase Inhibitors Biology Microbiology Article Cathepsin B Conserved sequence chemistry.chemical_compound Cell Wall Cathepsin H Animals Amino Acid Sequence Ciliophora Molecular Biology Peptide sequence Conserved Sequence Phylogeny Cathepsin Dose-Response Relationship Drug Sequence Homology Amino Acid Reverse Transcriptase Polymerase Chain Reaction Leupeptin Cell Differentiation Calpain Dipeptides General Medicine Protein Structure Tertiary Cysteine Endopeptidases Biochemistry chemistry biology.protein |
| Zdroj: | idUS. Depósito de Investigación de la Universidad de Sevilla instname |
| ISSN: | 1535-9786 1535-9778 |
| DOI: | 10.1128/ec.2.6.1234-1245.2003 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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