Figure 2: GEF-catalysed nucleotide exchange. | Nature Communications

Figure 2: GEF-catalysed nucleotide exchange.

From: Locking GTPases covalently in their functional states

Figure 2

(a) Rab1bWT, (b) Rab1E35C and (c) Rab1bL125C (black traces) non-covalently bound to GDP were mixed with an excess of GppNHp (Guanosine 5′-[β,γ-imido]triphosphate, step 1) and catalytic amounts of DrrA340-533 (DrrA-GEF, step 2). The nucleotide exchange reaction in step 2 was fitted with a single exponential equation yielding observed rate contants of 5.1 × 10−3 s−1 (Rab1WT), 7.5 × 10−3 s−1 (Rab1E35C) and 1.3 × 10−3 s−1 (Rab1L125C). In contrast to the non-covalently nucleotide-bound proteins, both Rab1 mutants containing the covalently bound nucleotides (green traces) did not show any nucleotide exchange upon addition of DrrA-GEF.

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