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• W2056553534 abstract "Gram-negative purple bacteria possess pairs of extracytoplasmic, ATP-independent, fimbrium-specific chaperone proteins which cooperatively function in the assembly of this extracellular organelle. The two non-homologous families of these proteins have been termed “Fimbrial chaperone family no. 1” (FCF1) and “Fimbrial chaperone family no. 2” (FCF2). The eleven sequenced or partially sequenced members of each of these two protein families were analysed. Their sequences were multiply aligned, and average similarity and hydropathy plots were generated. Statistical analyses of the sequences revealed that the short FCF1 proteins (of about 240 residues) have been better conserved through evolutionary time than have the much larger FCF2 proteins (of about 830 residues). Moreover, the N-terminal thirds of the FCF2 proteins are better conserved than the central or C-terminal thirds of these proteins. Phylogenetic tree construction revealed that, in general, the two proteins which cooperate in the assembly of a particular fimbrial type have similar positions on their respective phylogenetic trees, suggesting that the two proteins evolved in parallel as a functional unit. Two exceptions were noted, however. In one case, a hybrid protein appears to have arisen, possibly by genetic recombination. In another case, the two proteins of a particular pair may have evolved separately and come together late in the evolutionary process to provide their cooperative function. Les bactéries pourpres à Gram négatif portent des paires de protéines chaperons périplasmiques, ATP-indépendantes, spécifiques des fimbriae, et qui ont une fonction de coopération dans l'assemblage des organelles extracellulaires. Les deux familles non homologues de ces protéines ont été appelées FCF1 et FCF2 («fimbrial chaperone familieså 1 et 2). Les onze membres séquencés de ces deux familles de protéines ont été analysés. Leurs séquences ont été alignées et les similarités moyennes ainsi que les tracés ont été établis. Les analyses statistiques de séquences révélent que les protéines courtes FCF1 (environ 240 résidus) se sont mieux conservées au cours de l'évolution que les grandes protéines FCF2 (près de 830 résidus). De plus, les tiers N-terminaux des protéines FCF2 sont mieux conservés que les tiers centraux et C-terminaux. La construction d'un arbre phylogénique a révélé que les deux protéines qui coopèrent dans l'assemblage d'un type particulier de fimbriae ont généralement une position similaire dans leur arbre phylogénique respectif, ce qui suggère une évolution parallèle de ces deux protéines en tant qu'unités fonctionnelles. On note cependant deux exceptions: dans un des cas une portion hybride semble avoir émergée, possiblement par recombinaison génétique, et dans l'autre cas les deux protéines d'une paire particulière semblent avoir évolué separément pour se rencontrer tardivement dans le processus de l'évolution pour assurer leur fonction de coopération." @default.
• W2056553534 created "2016-06-24" @default.
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• W2056553534 date "1993-01-01" @default.
• W2056553534 modified "2023-10-16" @default.
• W2056553534 title "Structural and evolutionary relationships between two families of bacterial extracytoplasmic chaperone proteins which function cooperatively in fimbrial assembly" @default.
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• W2056553534 doi "https://doi.org/10.1016/0923-2508(93)90001-i" @default.
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