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ISBN-10: 0470514450

ISBN-13: 9780470514450

ISBN-10: 0471939145

ISBN-13: 9780471939146

Utilizing a multidisciplinary method, it positive aspects contributions and discussions of the most recent learn from top scientists engaged on all elements of GTPase job. Covers all identified participants of the real superfamily of enzymes--the GTPases. Considers quite a few key mobile services and the way they're regulated by means of GTPases. additionally describes a number of regulatory proteins that modulate GTPase task.

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Bosch, unpublished). At present therefore, we can only speculate about the function of these two proteins. It is attractive to think EF-Tu2 and 3 play a role during Streptomyces differentiation, analogous to that in Xenopus laevis: the similarity between the identity percentages within the two elongation factor groups is striking. In spores, however, the major product seems to be EF-Tul. EF-Tu2 or 3 might also be a minor factor for a special tRNA, because the transition to stage 2 is triggered by the expression of a rare tRNALeU,required for the translation of ‘late’ mRNAs.

6, 8 mM MgCl,, 60 mM NH,Cl and 7 mM 2-mercaptoethanol. GTPase activities were measured without (open symbols) or with (closed symbols) 30 pM AICI, and 1 mM NaF. Without ribosomes the GTPase activity of EF-G is undetectable. The background GTPase activity of ribosomes alone almost coincides with the closed squares. The interference of fluoroaluminates with EF-G, which occurs only when EF-G is in interaction with ribosomes, reminded us of the well-known effect of fusidic acid in such a system. Fusidic acid was therefore chosen as a reference in our study of stable complex formation between EF-G and the ribosome using nitrocellulose membrane filtration.

I should also mention that when we added inhibitors such as fusidic acid or fluoroaluminates, the synergistic effect disappeared. You just see the very small contribution of EF-Tu alone. But this doesn’t prove that it’s the EF-G GTPase centre that is inhibited; it’s just a possible conclusion. Eccleston: Is anything known about where EF-Ts binds on EF-Tu, for example, from expression of the isolated N- and C-terminal domains? Kraal: There is a mutant EF-Tu lacking the G domain (domain l), namely A(1-208) from Thermus thermophilus (see Table 2).

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Ciba Foundation Symposium 176 - The GTPase Superfamily


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