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Sequence analysis of bacterial redox enzyme maturation proteins (REMPs)

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The twin-arginine protein transport (Tat) system is a remarkable molecular machine dedicated to the translocation of fully folded proteins across energy-transducing membranes. Complex cofactor-containing Tat substrates acquire their cofactors prior to export, and substrate proteins actually require to be folded before transport can proceed. Thus, it is very likely that mechanisms exist to prevent wasteful export of immature Tat substrates or to curb competition between immature and mature substrates for the transporter. Here we assess the primary sequence relationships between the accessory proteins implicated in this process during assembly of key respiratory enzymes in the model prokaryote Escherichia coli. For each respiratory enzyme studied, a redox enzyme maturation protein (REMP) was assigned. The main finding from this review was the hitherto unexpected link between the Tat-linked REMP DmsD and the nitrate reductase biosynthetic protein NarJ. The evolutionary link between Tat transport and cofactor insertion processes is discussed.Key words: Tat translocase, twin-arginine leader, hydrogenase, nitrate reductase, TMAO reductase, DMSO reductase, formate dehydrogenase, Tor, Dms, Hya, Hyb, Fdh, Nap.

Le système de transport de protéines à arginines doubles (Tat) est une formidable machine moléculaire consacrée à la translocation de protéines complètement repliées au travers de membranes transmettant de l'énergie. Les substrats complexes de Tat contenant des cofacteurs acquièrent ceux-ci avant l'exportation; les substrats protéiques ont en fait besoin d'être repliés avant que le transport puisse se faire. Il est donc fort possible que des mécanismes existent afin d'empêcher une exportation inutile de substrats de Tat immatures ou de réduire la compétition entre les substrats matures et immatures pour le transporteur. Nous avons évalué dans cette étude les liens entre les séquences primaires et les protéines accessoires impliquées dans ce processus lors de l'assemblage d'enzymes respiratoires clés dans le modèle procaryotique de Escherichia coli. Une protéine de maturation d'enzymes rédox (PMER) a été attitrée à chaque enzyme étudiée. La découverte principale de cette enquête fut le lien jusqu'ici insoupçonné entre la PMER DmsD liée au Tat et la protéine biosynthétique et nitrate réductase NarJ. Le lien évolutif entre le transport Tat et le processus d'insertion des cofacteurs est débattu.Mots clés : translocase Tat, séquence de tête à arginine double, hydrogénase, nitrate réductase, TMAO réductase, DMSO réductase, formate déshydrogénase, Tor, Dms, Hya, Hyb, Fdh, Nap.[Traduit par la Rédaction]

Document Type: Research Article

Publication date: 2004-04-01

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  • Published since 1954, this monthly journal contains new research in the field of microbiology including applied microbiology and biotechnology; microbial structure and function; fungi and other eucaryotic protists; infection and immunity; microbial ecology; physiology, metabolism and enzymology; and virology, genetics, and molecular biology. It also publishes review articles and notes on an occasional basis, contributed by recognized scientists worldwide.
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