Discover protein sequence signatures from protein-protein interaction data

<p>Abstract</p> <p>Background</p> <p>The development of high-throughput technologies such as yeast two-hybrid systems and mass spectrometry technologies has made it possible to generate large protein-protein interaction (PPI) datasets. Mining these datasets for underlyi...

Full description

Bibliographic Details
Main Authors: Haasl Ryan J, Fang Jianwen, Dong Yinghua, Lushington Gerald H
Format: Article
Language:English
Published: BMC 2005-11-01
Series:BMC Bioinformatics
Online Access:http://www.biomedcentral.com/1471-2105/6/277
Description
Summary:<p>Abstract</p> <p>Background</p> <p>The development of high-throughput technologies such as yeast two-hybrid systems and mass spectrometry technologies has made it possible to generate large protein-protein interaction (PPI) datasets. Mining these datasets for underlying biological knowledge has, however, remained a challenge.</p> <p>Results</p> <p>A total of 3108 sequence signatures were found, each of which was shared by a set of guest proteins interacting with one of 944 host proteins in <it>Saccharomyces cerevisiae </it>genome. Approximately 94% of these sequence signatures matched entries in InterPro member databases. We identified 84 distinct sequence signatures from the remaining 172 unknown signatures. The signature sharing information was then applied in predicting sub-cellular localization of yeast proteins and the novel signatures were used in identifying possible interacting sites.</p> <p>Conclusion</p> <p>We reported a method of PPI data mining that facilitated the discovery of novel sequence signatures using a large PPI dataset from <it>S. cerevisiae </it>genome as input. The fact that 94% of discovered signatures were known validated the ability of the approach to identify large numbers of signatures from PPI data. The significance of these discovered signatures was demonstrated by their application in predicting sub-cellular localizations and identifying potential interaction binding sites of yeast proteins.</p>
ISSN:1471-2105