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Genome Biology

, 7:R45

First Online: 16 June 2006Received: 06 March 2006Revised: 04 April 2006Accepted: 27 April 2006


BackgroundMost proteins interact with only a few other proteins while a small number of proteins hubs have many interaction partners. Hub proteins and non-hub proteins differ in several respects; however, understanding is not complete about what properties characterize the hubs and set them apart from proteins of low connectivity. Therefore, we have investigated what differentiates hubs from non-hubs and static hubs party hubs from dynamic hubs date hubs in the protein-protein interaction network of Saccharomyces cerevisiae.

ResultsThe many interactions of hub proteins can only partly be explained by bindings to similar proteins or domains. It is evident that domain repeats, which are associated with binding, are enriched in hubs. Moreover, there is an over representation of multi-domain proteins and long proteins among the hubs. In addition, there are clear differences between party hubs and date hubs. Fewer of the party hubs contain long disordered regions compared to date hubs, indicating that these regions are important for flexible binding but less so for static interactions. Furthermore, party hubs interact to a large extent with each other, supporting the idea of party hubs as the cores of highly clustered functional modules. In addition, hub proteins, and in particular party hubs, are more often ancient. Finally, the more recent paralogs of party hubs are underrepresented.

ConclusionOur results indicate that multiple and repeated domains are enriched in hub proteins and, further, that long disordered regions, which are common in date hubs, are particularly important for flexible binding.

Electronic supplementary materialThe online version of this article doi:10.1186-gb-2006-7-6-r45 contains supplementary material, which is available to authorized users.

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Autor: Diana Ekman - Sara Light - Åsa K Björklund - Arne Elofsson

Fuente: https://link.springer.com/

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