Discover protein sequence signatures from protein-protein interaction data
Open Access
- 23 November 2005
- journal article
- Published by Springer Nature in BMC Bioinformatics
- Vol. 6 (1), 277
- https://doi.org/10.1186/1471-2105-6-277
Abstract
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. 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 Saccharomyces cerevisiae 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. We reported a method of PPI data mining that facilitated the discovery of novel sequence signatures using a large PPI dataset from S. cerevisiae 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.Keywords
This publication has 30 references indexed in Scilit:
- The evolution of domain arrangements in proteins and interaction networksCellular and Molecular Life Sciences, 2005
- The MIPS mammalian protein–protein interaction databaseBioinformatics, 2004
- The Database of Interacting Proteins: 2004 updateNucleic Acids Research, 2004
- Global analysis of protein localization in budding yeastNature, 2003
- Analyzing yeast protein–protein interaction data obtained from different sourcesNature Biotechnology, 2002
- Comparative assessment of large-scale data sets of protein–protein interactionsNature, 2002
- Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometryNature, 2002
- Functional organization of the yeast proteome by systematic analysis of protein complexesNature, 2002
- A comprehensive two-hybrid analysis to explore the yeast protein interactomeProceedings of the National Academy of Sciences, 2001
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983