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http://hdl.handle.net/1942/1612
Title: | Whole genome phage display selects for proline-rich Boi polypeptides against Bem1p | Authors: | Hertveldt, K. ROBBEN, Johan Volckaert, G. |
Issue Date: | 2006 | Publisher: | Springer | Source: | BIOTECHNOLOGY LETTERS, 28(16). p. 1233-1239 | Abstract: | 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 ~7.7 × 107 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. | Keywords: | Mass spectrometry - Phage display - Protein–protein interaction - Proteomics - Saccharomyces cerevisiae - SH3 domain | Document URI: | http://hdl.handle.net/1942/1612 | ISSN: | 0141-5492 | e-ISSN: | 1573-6776 | DOI: | 10.1007/s10529-006-9082-y | ISI #: | 000239085600003 | Category: | A1 | Type: | Journal Contribution | Validations: | ecoom 2007 |
Appears in Collections: | Research publications |
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