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| WILHELM,VIVIAN; HUARACÁN,BERNARDO; MARTÍNEZ,RODRIGO; ROSEMBLATT,MARIO; BURZIO,LUIS O; VALENZUELA,PABLO D.T. |
| The genes encoding the heat shock proteins HSP10 and HSP16 of the salmon pathogen Piscirickettsia salmonis have been isolated and sequenced. The HSP10 coding sequence is located in an open reading frame of 291 base pairs encoding 96 aminoacids. The HSP16 coding region was isolated as a 471 base pair fragment encoding a protein of 156 aminoacids. The deduced aminoacid sequences of both proteins show a significant homology to the respective protein from other prokaryotic organisms. Both proteins were expressed in E. coli as fusion proteins with thioredoxin and purified by chromatography on Ni-column. A rabbit serum against P. salmonis total proteins reacts with the recombinant HSP10 and HSP16 proteins. Similar reactivity was determined by ELISA using serum... |
| Tipo: Journal article |
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| Ano: 2003 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602003000300013 |
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| TISCHLER,NICOLE D; FERNÁNDEZ,JORGE; MÜLLER,ILSE; MARTÍNEZ,RODRIGO; GALENO,HÉCTOR; VILLAGRA,ELIECER; MORA,JUDITH; RAMÍREZ,EUGENIO; ROSEMBLATT,MARIO; VALENZUELA,PABLO D.T.. |
| We report here the complete genomic sequence of the Chilean human isolate of Andes virus CHI-7913. The S, M, and L genome segment sequences of this isolate are 1,802, 3,641 and 6,466 bases in length, with an overall GC content of 38.7%. These genome segments code for a nucleocapsid protein of 428 amino acids, a glycoprotein precursor protein of 1,138 amino acids and a RNA-dependent RNA polymerase of 2,152 amino acids. In addition, the genome also has other ORFs coding for putative proteins of 34 to 103 amino acids. The encoded proteins have greater than 98% overall similarity with the proteins of Andes virus isolates AH-1 and Chile R123. Among other sequenced Hantavirus, CHI-7913 is more closely related to Sin Nombre virus, with an overall protein... |
| Tipo: Journal article |
Palavras-chave: Hantavirus; Genome sequence; RNA polymerase; Human isolate. |
| Ano: 2003 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602003000200010 |
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| ARAYA,PAMELA; ROSEMBLATT,MARIO; VALENZUELA,PABLO; MURIALDO,HELIOS. |
| Lambda DNA terminase, the enzyme that cleaves virion-length chromosomes from multigenomic concatemers and packages them into the bacteriophage head, is composed of two subunits, gpNu1 and gpA. Direct determination of the structure of gpNu1, the smaller subunit, has not been possible because of its insolubility in aqueous solutions. Therefore, to identify smaller and potentially water-soluble domains of gpNu1, we analyzed the nature of the products obtained by limited digestion of the protein with several proteases. The gpNu1 subunit was obtained from E.coli cells transfected with the plasmid pH6-Nu1 that overproduces the protein. Incubation of gpNu1 solubized in 2.5 M guanidinium chloride with chymotrypsin resulted in the formation of at least eight... |
| Tipo: Journal article |
Palavras-chave: DNA packaging; Terminase; GpNu1 structural domains; Limited proteolysis. |
| Ano: 2001 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602001000300008 |
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