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Sci. STKE, 31 May 2005
Vol. 2005, Issue 286, p. re7
[DOI: 10.1126/stke.2862005re7]

REVIEWS

The Many Faces of SAM

Feng Qiao and James U. Bowie*

University of California, Los Angeles–U.S. Department of Energy (UCLA-DOE) Institute of Genomics and Proteomics, Molecular Biology Institute, Department of Chemistry and Biochemistry, UCLA, CA 90095, USA.

Gloss: Cells need to make appropriate responses to complex signals. One way in which they accomplish this task is by constructing large complexes of macromolecules, bringing together various sensors and effectors that facilitate the integration of input and output. Proteins are often brought into these macromolecular complexes by small modules that have specialized binding properties. The process of evolution can move these modules to different proteins, thereby conferring the distinctive binding properties of the module to new proteins. One particularly versatile protein module is called a SAM domain. SAM domains can associate into long strings containing many SAM domains or into small clusters of only a few SAM domains; they can bind to many different proteins, and they can also bind to RNA. It seems likely that some SAM domains could also provide functions that we do not yet know about. Efforts to learn about these additional functions continue. Ultimately, we would like to know how to predict the function of any SAM domain.

*Corresponding author. Department of Chemistry and Biochemistry, Room 655, Boyer Hall, UCLA, 611 Charles E. Young Drive East, Los Angeles, CA 90095–1570, USA. E-mail: bowie{at}mbi.ucla.edu

Citation: F. Qiao, J. U. Bowie, The Many Faces of SAM. Sci. STKE 2005, re7 (2005).

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