Summary: Era, an essential GTPase, is present in many bacteria and spp. and appears to play a major role in the cell cycle and other cellular processes. To further understand its function, an gene from was identified and cloned, and a mutant gene with a deletion of 68 codons from its 3′-terminus was constructed. The truncated Era protein was then purified and characterized, and the ability of the truncated gene to complement an mutant strain defective in Era production was examined. Like the full-length Era protein, the truncated Era protein was able to bind and hydrolyse GTP, but its binding activity was increased twofold and its hydrolytic activity was reduced sevenfold when compared with those of the full-length Era protein. Unlike the full-length Era protein, the truncated Era protein lost its ability to bind to the cytoplasmic membrane. The full-length gene was able to complement the mutant deficient in Era production when carried on pACYC184, while the truncated gene failed to do so when carried on pACYC184, pBR322 or pUC18. The cellular amounts of the truncated Era and the full-length Era proteins in and respectively, were then determined by Western blot analysis. In addition, the minimal amount of the Era protein needed for complementation of the mutant was also measured. Taken together, these results suggest that the C-terminus of the Era protein might be responsible for the binding of the protein to the cytoplasmic membrane and be essential for function.


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