Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1940873 | Biochemical and Biophysical Research Communications | 2006 | 6 Pages |
Abstract
Bacteria encode a number of relatively poorly characterized GTPases, including the essential, ribosome-associated Obg/CgtA proteins. In contrast to Ras-like proteins, it appears that the Obg/CgtA proteins bind guanine nucleotides with modest affinity and hydrolyze GTP relatively slowly. We show here that the Vibrio harveyi CgtAV exchanges guanine nucleotides rapidly and has a modest affinity for nucleotides, suggesting that these features are a universal property of the Obg/CgtA family. Interestingly, CgtAV possesses a significantly more rapid GTP hydrolysis rate than is typical of other family members, perhaps reflecting the diversity and specificity of bacterial ecological niches.
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Authors
A.E. Sikora, K. Datta, J.R. Maddock,