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- W2016458593 abstract "The transmembrane histidine kinase VirA is responsible for the recognition of information from several plant-derived xenognostic signals that control gene transfer between Agrobacterium tumefaciens and its eukaryotic host. As with other histidine autokinases, VirA appears to exist as a homodimer within the inner membrane of the bacterium. In this study, we identify the putative homodimeric coiled-coil-like motifs Helix TM2 (amino acids (aa) 259-288) and Helix C (aa 293-327) within the previously assigned signal input domain. The functional importance of these coiled-coil interactions in signal-mediated VirA activation is investigated by the construction of fusion proteins with the leucine zipper domain of the transcription factor GCN4. Replacement of the membrane-spanning and periplasmic domains of VirA with the GCN4 leucine zipper gave functional proteins with increased signal-induced vir gene expression. When the GCN4 fusion was used to conformationally bias the interface of the Helix C coiled coil, constitutively active chimeras were created. The activity of these constructs was dependent on the interface of the Helix C coiled coil, and a ratchet model is proposed in which VirA activation is achieved by signal-induced switching of the interfaces of the homodimer. Since VirA functions as a transducer and integrates various host cues indirectly, these data highlight its role as an antenna for the tumor-inducing (Ti) plasmid, able to monitor the host proteome so as to select for successful xenognostic signaling strategies." @default.
- W2016458593 created "2016-06-24" @default.
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- W2016458593 date "2002-04-02" @default.
- W2016458593 modified "2023-10-13" @default.
- W2016458593 title "Ratcheting Upvir Gene Expression inAgrobacterium tumefaciens: Coiled Coils in Histidine Kinase Signal Transduction" @default.
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- W2016458593 doi "https://doi.org/10.1002/1439-7633(20020402)3:4<311::aid-cbic311>3.0.co;2-n" @default.
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