Here we present an AP-MS survey of the bacterium Desulfovibrio vulgaris. We have identified 459 high confidence PPIs from D. vulgaris. Compared to the nine published interactomes, our two networks are smaller; are much less highly connected; have significantly lower false discovery rates; and are much more enriched in protein pairs that are encoded in the same operon, have similar functions, and are reproducibly detected in other physical interaction assays. Our work establishes more stringent benchmarks for the properties of protein interactomes and suggests that bona fide PPIs much more frequently involve protein partners that are annotated with similar functions or that can be validated in independent assays than earlier studies suggested.
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: protein-protein interactions, AP-MS, tandem affinity purification, Desulfovibrio vulgaris
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Gareth Butland |
Submitting User: | halinaewa |
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