Novel properties of bacterial elongation factor Tu.

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Abstract
Novel properties of the bacterial protein synthesis elongation factor Tu are characterized indicating that it may function as a structural protein. Under appropriate conditions, elongation factor Tu polymerizes to form filaments and, more often, bundles of filaments. It is also the predominant component of a complex of proteins from Escherichia coli that undergoes reversible polymerization in the presence of KCl and MgCl2. Purified elongation factor Tu binds tightly to DNase I in the presence of 10 mM MgCl2. In crude extracts the factor shows no binding in the presence or absence of MgCl2. Elongation factor Tu may have certain actin-like properties and that it has cellular functions other than its role protein synthesis.