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 | Gianni Cesareni - |  |
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A substantial fraction of the protein network is based on interactions
mediated by small protein recognition modules binding to short peptides
in the partner proteins. However, the number of interactions mediated
by each domain and the degree of promiscuity at a whole proteome level
has not been investigated. Most of these interactions are transient and
cannot be easily detected by co-purification experiments.
I will describe strategies to reliably detect these interactions
on a genomic scale We have used a combination of phage display and
positionally addressed peptide synthesis (PepSPOT) to screen all the
peptides in the yeast proteome for their potential to bind several
different SH3 domains.The same approach, that we have named WISE
(Whole Interactome Scanning Experiment), was exploited to screen all
the phosphopeptides in the yeast proteome for their ability to bind
the two isophorms of the yeast 14-3-3 proteins.
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