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. 2013 May 24;52(23):4105. doi: 10.1021/bi4006094

Correction to Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases

Andrew M Sydor, Marco Jost, Katherine S Ryan, Kaitlyn E Turo, Colin D Douglas, Catherine L Drennan , Deborah B Zamble
PMCID: PMC3680914

An error has been found in Table 2. The exponent for kcat of apo WT-YjiA should be 10–4, not 10–3. This change does not impact any of the findings in the paper because the conclusions were based on the reported kcat/Km, which is correct. The revised, corrected table is shown below.

Table 2. Kinetics of GTP Hydrolysis by WT and E37A,C66A,C67A YjiAa.

YjiA variant metal bound kcat (s–1) Km (M) kcat/Km (M–1 s–1)
WT apo (6 ± 2) × 10–4 (5 ± 3) × 10–5 14 ± 9
  Co(II) (5 ± 2) × 10–4 (2.3 ± 0.7) × 10–4 2.3 ± 0.8
  Ni(II)   WHb  
  Zn(II)   NHc  
E37A,C66A,C67A apo (5 ± 1) × 10–4 (1.0 ± 0.7) × 10–4 6 ± 3
  Co(II) (1.1 ± 0.1) × 10–3 (1.7 ± 0.1) × 10–5 78 ± 9
  Ni(II) (6 ± 1) × 10–4 (3 ± 1) × 10–4 2 ± 1
  Zn(II)   NHc  
a

All GTPase assays were conducted with 0.5–2 μM WT or E37A,C66A,C67A YjiA in protein buffer supplemented with 5 mM MgCl2. Samples containing metal were preincubated with either zinc, cobalt, or nickel overnight at 4 °C in an anaerobic glovebox. The amount of released phosphate was detected using a modified Malachite Green assay. The data listed are average values from at least three independent experiments.

b

WH, weak hydrolysis (see main text for details).

c

NH, no measurable hydrolysis.


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