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. 2012 Oct 3;31(19):3949–3950. doi: 10.1038/emboj.2012.245

Mechanism of nucleotide sensing in group II chaperonins

Jose H Pereira, Corie Y Ralston, Nicholai R Douglas, Ramya Kumar, Tom Lopez, Ryan P McAndrew, Kelly M Knee, Jonathan A King, Judith Frydman, Paul D Adams
PMCID: PMC3463849

Correspondence to: pdadams@lbl.gov

Correction to: The EMBO Journal (2012) 31, 731–740. doi: 10.1038/emboj.2011.468

Since the publication of this article, the authors have discovered that in Figure 4B and Supplementary Figure S3B there is an error in the units reported on the y axes. In both cases, the units should read pmol/μl (i.e., picomoles per microlitre).

Figure 4.

Figure 4

(A) PK digestion of Cpn-WT, Cpn-G160S, Cpn-K161A and Cpn-E164A mutants, analysed by SDS–PAGE followed by Coomassie blue staining. PK leads to full digestion of the open Cpn lids. Incubation with ATP–AlFx locks the complex closed leading to complete PK protection of lids (compare ATP free and +ATP AlFx lanes). (B) ATP hydrolysis by Cpn-WT, Cpn-G160S, Cpn-K161A and Cpn-E164A measured at 1 and 2 mM of α-[32P]-ATP. (C) ATP hydrolysis by Cpn-G160S and the catalytic dead mutant Cpn-D386A measured at 1 mM α-[32P]-ATP. The mean with the error bars representing standard error of the mean (s.e.m.) is shown. (D) Filter-binding assays for Cpn-WT, Cpn-G160S, Cpn-K161A and Cpn-E164A. Shown is the mean, with the error bars representing s.e.m. Data shown in (C, D) are the result of three independent repeats.

The correct Figure 4 is shown here and the Supplementary File has been corrected online.

The authors apologise for any inconvenience caused.

Supplementary Material

Supplementary data
emboj2012245s1.doc (3.3MB, doc)

Associated Data

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Supplementary Materials

Supplementary data
emboj2012245s1.doc (3.3MB, doc)

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