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Gastric interactions

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Large numbers of protein-protein interactions have been mapped for yeast and worms, and now in the January 11 Nature, Rain et al. present the first large set of interactions for a prokaryote (Nature 2001, 409:211-215). The two-hybrid screen of 261 proteins from the gastric pathogen Heliobacter pylori against a library of genome-encoded polypeptides revealed 1,200 putative interactions. Screening against a library allows the identification of interacting domains, and reduces the rate of false negatives encountered in classical pair-wise screens. A strong selection protocol reduces the number of false positives. Rain et al. also use a probability score to compute the likelihood that a given two-hybrid result is a consequence of background noise, and use some of the identified interactions to assign various proteins to particular biological pathways.

References

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    A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae.

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    Protein interaction mapping in C. elegans using proteins involved in vulval development.

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    Nature, [http://0-www.nature.com.brum.beds.ac.uk/nature/]

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Wells, W. Gastric interactions. Genome Biol 2, spotlight-20010117-01 (2001) doi:10.1186/gb-spotlight-20010117-01

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Keywords

  • Polypeptide
  • False Positive
  • False Negative
  • Background Noise
  • Biological Pathway