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| Khater,Letícia; Santos,Túlio M.; Alegria,Marcos C.; Docena,Cassia; Silva,Ana C.R. da; Ramos,Carlos H.I.. |
| The secretion of bacterial virulence factors and flagellar components requires the assistance of specific type III and flagellar chaperones. Standard computational annotation of the genome of Xanthomonas axonopodis pv citri, a plant pathogen that causes citrus canker, initially did not identify any genes belonging to these chaperone categories since the primary sequence homology between them was very low. However, in a search for hypothetical proteins with characteristics similar to these chaperones, we have now identified 30 chromosomal and 10 plasmidial potential genes encoding chaperones belonging to types III/IV, and flagellar secretion systems in this organism. The significance of these findings is discussed. |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Chaperone; Protein secretion; Type III and type IV secretion systems; Xanthomonas. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572005000200024 |
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| Cagliari,Thiago C.; Tiroli,Ana O.; Borges,Júlio C.; Ramos,Carlos H.I.. |
| Expressed Sequence Tags (ESTs) sequencing provides reliable and useful information concerning gene expression patterns in the genomic context. Our group used bioinformatics to identify and annotate 5'EST-contigs belonging to the molecular chaperones within the Eucalyptus Genome Sequencing Project Consortium (FORESTs) database. We found that 1,959 5'EST-contigs, or approximately 1.6% of the total 5'EST-contigs, encoded chaperones, emphasizing their biological importance. About 55% of the chaperones that we found were Hsp70 chaperones and its co-chaperones, 18% were Hsp90 chaperones, 15% were Hsp60 and its co-chaperone, 8% were Hsp100 chaperones, and 4% were Small Hsps. We also investigated the digital expression profile of the chaperone genes to gain... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Chaperones; Heat shock proteins; Genome; Expressed sequence tags. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572005000400006 |
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| Borges,Júlio C.; Peroto,Maria C.; Ramos,Carlos H.I.. |
| Some newly synthesized proteins require the assistance of molecular chaperones for their correct folding. Chaperones are also involved in the dissolution of protein aggregates making their study significant for both biotechnology and medicine and the identification of chaperones and stress-related protein sequences in different organisms is an important task. We used bioinformatic tools to investigate the information generated by the Sugarcane Expressed Sequence Tag (SUCEST) genome project in order to identify and annotate molecular chaperones. We considered that the SUCEST sequences belonged to this category of proteins when their E-values were lower than 1.0e-05. Our annotation shows that 4,164 of the 5 expressed sequence tag (EST) sequences were... |
| Tipo: Info:eu-repo/semantics/article |
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| Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572001000100013 |
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| Mokry,David Z.; Abrahão,Josielle; Ramos,Carlos H.I.. |
| The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Amyloid; Disaggregase; Shock protein; Molecular chaperones; Prion; Protein folding. |
| Ano: 2015 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000301273 |
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