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- W2128792330 abstract "One of the most promising methods for large-scale studies of protein interactions is isolation of an affinity-tagged protein with its in vivo interaction partners, followed by mass spectrometric identification of the copurified proteins. Previous studies have generated affinity-tagged proteins using genetic tools or cloning systems that are specific to a particular organism. To enable protein−protein interaction studies across a wider range of Gram-negative bacteria, we have developed a methodology based on expression of affinity-tagged “bait” proteins from a medium copy-number plasmid. This construct is based on a broad-host-range vector backbone (pBBR1MCS5). The vector has been modified to incorporate the Gateway DEST vector recombination region, to facilitate cloning and expression of fusion proteins bearing a variety of affinity, fluorescent, or other tags. We demonstrate this methodology by characterizing interactions among subunits of the DNA-dependent RNA polymerase complex in two metabolically versatile Gram-negative microbial species of environmental interest, Rhodopseudomonas palustris CGA010 and Shewanella oneidensis MR-1. Results compared favorably with those for both plasmid and chromosomally encoded affinity-tagged fusion proteins expressed in a model organism, Escherichia coli." @default.
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- W2128792330 date "2008-07-01" @default.
- W2128792330 modified "2023-09-26" @default.
- W2128792330 title "A General System for Studying Protein−Protein Interactions in Gram-Negative Bacteria" @default.
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- W2128792330 doi "https://doi.org/10.1021/pr8001832" @default.
- W2128792330 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18590317" @default.
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