An essential component of all type III secretion systems is a highly conserved ATPase that shares significant amino acid sequence similarity to the beta subunit of the F0F1 ATPases and is thought to provide the energy for the secretion process. We have performed a genetic and functional analysis of InvC, the ATPase associated with the Salmonella enterica type III secretion system encoded within its pathogenicity island 1. Through a mutagenesis analysis, we have identified amino acid residues that are essential for specific activities of InvC, such as nucleotide hydrolysis and membrane binding. This has allowed us to define discrete domains of InvC that are specifically associated with different essential activities of this protein.
机构:
Catholic Univ Louvain, Microbial Pathogenesis Unit, Christian de Duve Inst Cellular Pathol, B-1200 Brussels, BelgiumCatholic Univ Louvain, Microbial Pathogenesis Unit, Christian de Duve Inst Cellular Pathol, B-1200 Brussels, Belgium
Cornelis, GR
Van Gijsegem, F
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机构:Catholic Univ Louvain, Microbial Pathogenesis Unit, Christian de Duve Inst Cellular Pathol, B-1200 Brussels, Belgium
机构:
Catholic Univ Louvain, Microbial Pathogenesis Unit, Christian de Duve Inst Cellular Pathol, B-1200 Brussels, BelgiumCatholic Univ Louvain, Microbial Pathogenesis Unit, Christian de Duve Inst Cellular Pathol, B-1200 Brussels, Belgium
Cornelis, GR
Van Gijsegem, F
论文数: 0引用数: 0
h-index: 0
机构:Catholic Univ Louvain, Microbial Pathogenesis Unit, Christian de Duve Inst Cellular Pathol, B-1200 Brussels, Belgium