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. D'une-façon-intéressante, cette boucle présente le même repliement dans la structure de XcpTG

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, To allocate each identified residues, a possible role in HPP formation and/or Xcp-dependent secretion, we gradually reintroduced in HxcT the nine corresponding residues found in XcpT. The reconstruction was performed by sequentially introducing each one of the nine substitutions in HxcT. The order by which the substitutions were introduced was driven by the predicted importance of these residues in the pseudopilus assembly. More precisely, in our reconstituted pseudopilus, the N-terminal part of the ?-helix of major pseudopilins is nearly parallel to the fiber axis in the center of the filament creating the hydrophobic core crucial for pseudopilus assembly. Therefore, residues located in this ?-helix and residues found at the interface between two neighboring XcpT and therefore possibly involved in intersubunit interaction were the first selected for the "gradual" directed mutagenesis. Moreover, mutation n1 was chosen first because it is located in the N-terminal ?-helix which has a FIGURE 1. HxcT and XcpT are not interexchangeable. A, 12% SDS-PAGE stained with Coomassie Brilliant Blue of supernatant fractions. Molecular mass markers are indicated on the left side of the gel. Some of the Xcp-(PmpA, ExoA, LasB, and PrpL) and the Hxc-(LapA) dependent substrates are indicated by arrows on the right side. B, phenotypical plate assays revealing Xcp-dependent secretion and activities of substrates. Proteolytic activity is shown by a halo around the colony on a skimmed milk plate (second column). Secretion of the lipase LipA is revealed by the growth of P. aeruginosa strains on a lipid agar plate, for T2SS-dependent secretion of exoenzymes (24, 25). However, XcpT cannot replace HxcT for LapA secretion in P. aeruginosa (Fig. 1A, lane 3). Importantly, heterologous complementation studies performed in K. oxytoca have shown that the major pseudopilins, XcpT from P. aeruginosa, vol.23

, Selection criteria for mutations of HxcT. A, sequence alignment of matured major pseudopilins from T2SSs. Sequence of HxcT from the T2SS of P. aeruginosa PAO1 is boxed. Identical residues are highlighted in black, conserved residues are highlighted in dark gray, and similar residues are highlighted in light gray. The secondary structure elements are indicated below the sequence alignment where cylinders represent the ?-helices, arrows represent the ?-strand, and the red line indicates the ??-loop region. The point mutations selected to transform HxcT in XcpT are indicate by asterisks

P. Ppu,

E. Eco,

E. Ech and . Chrysanthemi,

K. Kox,

V. Vch, MZO-3 (gi 153802200/ZP_01956786)

A. Ahy, N-terminal helix is colored in blue, ??-loop region in red, and the C-terminal three-stranded ?-sheet is colored in green, hydrophila ATCC 7966 (gi 117620343/YP_855105); and Pae, P. aeruginosa PAO1 (gi 15598297/NP_251791 and 15595878/ NP_249372) for XcpT and HxcT, respectively. B, ribbon view of the XcpT pseudopilin from P. aeruginosa (PAO1)

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