1995
DOI: 10.1021/bi00039a007 View full text |Buy / Rent full text
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Abstract: Transient kinetic experiments on the interaction of nucleotide-free EF-Tu from Thermus thermophilus with nucleotides using intrinsic protein fluorescence, extrinsic nucleotide fluorescence and fluorescence resonance energy transfer show that nucleotide binding is in general at least a two-step process. The first step is a weak initial binding, which is followed by a relatively slow isomerization of the protein-nucleotide complex in which changes of both intrinsic and extrinsic fluorescence, as well as energy t… Show more

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“…3b, the slope decreases at higher concentrations, and the dependence can be well described by a hyperbolic equation. This behavior is similar to that seen with other GTPases, including Ras (17), EF-Tu (18), and Rab5 or Rab7 (19), and has been interpreted as arising from a two-step binding mechanism as shown in Scheme 1:…”
Section: Resultssupporting
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“…3b, the slope decreases at higher concentrations, and the dependence can be well described by a hyperbolic equation. This behavior is similar to that seen with other GTPases, including Ras (17), EF-Tu (18), and Rab5 or Rab7 (19), and has been interpreted as arising from a two-step binding mechanism as shown in Scheme 1:…”
Section: Resultssupporting
“…Other GTPases that have been investigated at this level all show at least two-step binding of nucleotides. The association kinetics of GDP with FtsY initially appear very similar to those of Ras (17), EF-Tu (18), and Rab (19), with a weak but rapid initial binding step being followed by a relatively slow isomerization reaction. The rates of this step (k ϩ2 in Scheme 1) are approximately 20 s Ϫ1 (Ras), 400 s Ϫ1 (EF-Tu), and 80 s Ϫ1 (Rab7), compared with 119 s Ϫ1 for FtsY.…”
Section: Discussionmentioning
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“…The nucleotides dissociate from the Rasrelated nuclear G-protein slowly, with rate constants of 1.2 ϫ 10 Ϫ5 and 1.4 ϫ 10 Ϫ5 s Ϫ1 , respectively (23,24). Slow dissociation (0.85 ϫ 10 Ϫ3 s Ϫ1 for GDP and 5 ϫ 10 Ϫ3 s Ϫ1 for GTP) was observed also for elongation factor Tu from Thermus thermophilus (18). The slow dissociation in these proteins may suggest a common occluded state of nucleotide in the binding pocket following conformational rearrangement in the protein.…”
Section: Discussionmentioning
“…The nucleotide binding of ADP-ribosylated EF-Tu to mant-GTP, a fluorescent GTP derivative, was studied by using fluorescence resonance energy transfer from Trp184 in EF-Tu (27). Binding of the nucleotide to native or ADP-ribosylated EF-Tu increased mant-GTP fluorescence.…”
Section: Binding Of Mant-gtp To Adp-ribosylated Ef-tu Is Not Alteredmentioning