BACTERIAL PROTEINS MAPPED OUT
The first protein–protein interaction map of a bacterium is reported in Nature (Vol. 409, No. 6817, 11 Jan 2001, pp. 211–215) this week. Pierre Legrain, of the functional proteomics company Hybrigenics, in Paris, France, and colleagues have identified and mapped some 1,200 interactions between proteins from Helicobacter pylori, a common, ulcer-causing human gut bacterium.
The interactions connect almost half of the bacteria’s ‘proteome’: the full protein set expressed by its genome. Finding out what such proteins do — and how they do it — will put flesh on the bare bones of the decoded genomes of everything from H. pylori to humans.
Legrain’s team screened 261 H. pylori ‘bait’ proteins against a much larger collection of ‘prey’ protein fragments. Both bait and prey were expressed inside yeast, which are modified to grow only if the two molecules interact. Analysing the yeast colonies produced has already revealed which H. pylori proteins combine during urease synthesis, essential for the bug’s pathogenesis.
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