Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 30 April 2002
Vol. 2002, Issue 130, p. tw160
[DOI: 10.1126/stke.2002.130.tw160]

EDITORS' CHOICE

Protein Interactions Slowly Changing Partners

A wealth of genomic and proteomic information now makes it possible to analyze fundamental properties and evolution of protein interaction networks. To estimate evolutionary rates, Fraser et al. compared putative orthologous proteins in Saccharomyces cerevisiae and Caenorhabditis elegans. As expected, given that highly interactive proteins are more likely than their less-connected counterparts to be required for viability, highly connected proteins also appear to evolve more slowly. However, the authors' analysis indicates that what limits evolutionary rates of interacting proteins is that a greater proportion of the molecules themselves takes part in physical interactions. Changes in interacting partners are expected to be maintained only if a reciprocal change in the other partner also occurs. This requirement appears to require similar evolutionary rates for the interacting partners.

H. B. Fraser, A. E. Hirsh, L. M. Steinmetz, C. Scharfe, M. W. Feldman, Evolutionary rate in the protein interaction network. Science 296, 750-752 (2002). [Abstract] [Full Text]

Citation: Slowly Changing Partners. Sci. STKE 2002, tw160 (2002).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882