Difference between revisions of "Team:Aix-Marseille/Basic Part"
(→fliC E. coli, flagellin C coding sequence (BbaK1951005)) |
(→fliC Desulfovibrio, flagellin C coding sequence (BbaK1951006)) |
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This coding sequence codes the Flagellin C (FliC) protein from ''Escherichia coli'' strain. FliC is the main protein constitutive of the flagelar filament and is involved to promote bacterial swimming. This sequence is conserved in many bacterial strains. It has been demonstrated that Flagellin C has the ability to adsorb precious metal such as platinum or gold. | This coding sequence codes the Flagellin C (FliC) protein from ''Escherichia coli'' strain. FliC is the main protein constitutive of the flagelar filament and is involved to promote bacterial swimming. This sequence is conserved in many bacterial strains. It has been demonstrated that Flagellin C has the ability to adsorb precious metal such as platinum or gold. | ||
| − | ===fliC Desulfovibrio, flagellin C coding sequence | + | ==='''fliC ''Desulfovibrio'', flagellin C coding sequence''' [http://parts.igem.org/Part:BBa_K1951006 BBa_K1951006]=== |
| − | This coding sequence codes flagellin C which is a main protein involved for the extracellular flagellar establishment. Flagellar enables bacterial swimming. It has been shown that the flagellin structure from Desulfovibrio vulgaris strain Hildenborough can adsorb metallic nanoparticules as gold | + | This coding sequence codes flagellin C which is a main protein involved for the extracellular flagellar establishment. Flagellar enables bacterial swimming. It has been shown that the flagellin structure from ''Desulfovibrio vulgaris'' strain Hildenborough can adsorb metallic nanoparticules as gold or platinum. |
=== CsgA, curlin coding sequence (BbaK1951007)=== | === CsgA, curlin coding sequence (BbaK1951007)=== | ||
CsgA is the major and structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli are the major proteinaceous component of a complex extracellular matrix produced by many Enterobacteriaceae. Curli were first discovered in the late 1980s on Escherichia coli strains that caused bovine mastitis, and have since been implicated in many physiological and pathogenic processes of E. coli and Salmonella spp. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation. Curli also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response. | CsgA is the major and structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli are the major proteinaceous component of a complex extracellular matrix produced by many Enterobacteriaceae. Curli were first discovered in the late 1980s on Escherichia coli strains that caused bovine mastitis, and have since been implicated in many physiological and pathogenic processes of E. coli and Salmonella spp. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation. Curli also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response. | ||
