Whole genome phage display selects for proline-rich Boi polypeptides against Bem1p.
Interaction selection by biopanning from a fragmented yeast proteome displayed on filamentous phage particles was successful in identifying proline-rich fragments of Boi1p and Boi2p. These proteins bind to the second "src homology region 3'' (SH3) domain of Bem1p, a protein of Saccharomyces cerevisiae involved in bud formation. Target Bem1p was ... a doubly-tagged recombinant, Bem1([Asn142-Ile551]), which strongly interacts in ELISA with a C-terminal 75 amino acids polypeptide from Cdc24p exposed on phage. The whole yeast genomic display library contained approximately 7.7 x 10(7) independent clones of sheared S. cerevisiae genomic DNA fused to a truncated M13 gene III. This study corroborates the value of fragmented-proteome display to identify strong and direct interacting protein modules.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Cell Cycle Proteins, Genome, Fungal, Guanine Nucleotide Exchange Factors, Mass Spectrometry, Molecular Sequence Data, Peptide Library, Peptides, Proline, Protein Structure, Tertiary, Proteomics, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, src Homology Domains
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Cell Cycle Proteins, Genome, Fungal, Guanine Nucleotide Exchange Factors, Mass Spectrometry, Molecular Sequence Data, Peptide Library, Peptides, Proline, Protein Structure, Tertiary, Proteomics, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, src Homology Domains
Biotechnol. Lett.
Date: Aug. 01, 2006
PubMed ID: 16802101
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