Registrera dig | Logga in | FAQ      [?] 
CiteULike is a free online bibliography manager. Register and you can start organising your references online.
Recent | Unread | Search | Authors | Tags | Export

Global investigation of protein-protein interactions in yeast Saccharomyces cerevisiae using re-occurring short polypeptide sequences

by: S Pitre, C North, M Alamgir, M Jessulat, A Chan, X Luo, JR Green, M Dumontier, F Dehne, A Golshani
Nucl. Acids Res. (27 June 2008), gkn390.


View FullText article


X Reviews [Write a review of this article]

There are no reviews of this article

X Find related articles from these CiteULike users

X Find related articles with these CiteULike tags

X Referat

Protein-protein interaction (PPI) maps provide insight into cellular biology and have received considerable attention in the post-genomic era. While large-scale experimental approaches have generated large collections of experimentally determined PPIs, technical limitations preclude certain PPIs from detection. Recently, we demonstrated that yeast PPIs can be computationally predicted using re-occurring short polypeptide sequences between known interacting protein pairs. However, the computational requirements and low specificity made this method unsuitable for large-scale investigations. Here, we report an improved approach, which exhibits a specificity of [~]99.95% and executes 16 000 times faster. Importantly, we report the first all-to-all sequence-based computational screen of PPIs in yeast, Saccharomyces cerevisiae in which we identify 29 589 high confidence interactions of [~]2 x 107 possible pairs. Of these, 14 438 PPIs have not been previously reported and may represent novel interactions. In particular, these results reveal a richer set of membrane protein interactions, not readily amenable to experimental investigations. From the novel PPIs, a novel putative protein complex comprised largely of membrane proteins was revealed. In addition, two novel gene functions were predicted and experimentally confirmed to affect the efficiency of non-homologous end-joining, providing further support for the usefulness of the identified PPIs in biological investigations. 10.1093/nar/gkn390


X BibTeX record

X RIS record



RIS BibTeX