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Published Erratum
. 2023 Jan 3;120(1):e2220845120.
doi: 10.1073/pnas.2220845120. Epub 2022 Dec 28.

Correction for Couthouis et al., A yeast functional screen predicts new candidate ALS disease genes

No authors listed
Published Erratum

Correction for Couthouis et al., A yeast functional screen predicts new candidate ALS disease genes

No authors listed. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 4.
Fig. 4.
TAF15 is an aggregation-prone protein like TDP-43 and FUS. (A) Following TEV protease cleavage to remove the N-terminal GST tag, FUS, TAF15, and TDP-43 proteins were processed for SDS-PAGE and Coomassie stained to confirm purity and expected molecular weight. (B) GST-TDP-43, GST-FUS, or GST-TAF15 (3 μM) were incubated in the presence or absence of TEV protease at 25 °C for 0 to 90 min with agitation. Note that very little aggregation occurs in the absence of TEV protease. The extent of aggregation was determined by turbidity. Values represent means ± SEM (n = 3). (C) GST-TDP-43, GST-FUS, or GST-TAF15 (3 μM) was incubated in the presence of TEV protease at 25 °C for 0 to 60 min. At the indicated times, reactions were processed for sedimentation analysis. Pellet and supernatant fractions were resolved by SDS-PAGE and stained with Coomassie Brilliant Blue. The amount of protein in the pellet fraction was determined by densitometry in comparison with known quantities of the appropriate protein. Values represent means ± SEM (n = 3). A human RRM protein, DND1, which did not aggregate and was not toxic in yeast (Fig. 1 C and D), was also soluble and did not form aggregates in this assay. (D) GST-TDP-43, GST-FUS, or GST-TAF15 (3 μM) was incubated in the presence of TEV protease at 25 °C for 0 to 60 min. At various times, reactions were processed for EM. Small arrows denote small pore-shaped oligomers, and large arrows denote linear polymers. (Scale bar, 500 nm.) (E) Gallery of TDP-43, FUS, and TAF15 oligomers formed during aggregation reactions. (Scale bar, 50 nm.) (F) Following TEV protease cleavage to remove the N-terminal GST tag, TAF15 wild-type (WT), G391E, and R408C proteins were processed for SDS-PAGE and Coomassie stained to confirm purity and expected molecular weight. (G) ALS-linked TAF15 variants G391E and R408C displayed accelerated aggregation kinetics, whereas the R388H variant found in both cases and controls aggregated with similar kinetics to WT TAF15.
See this image and copyright information in PMC

Erratum for

  • A yeast functional screen predicts new candidate ALS disease genes.
    Couthouis J, Hart MP, Shorter J, DeJesus-Hernandez M, Erion R, Oristano R, Liu AX, Ramos D, Jethava N, Hosangadi D, Epstein J, Chiang A, Diaz Z, Nakaya T, Ibrahim F, Kim HJ, Solski JA, Williams KL, Mojsilovic-Petrovic J, Ingre C, Boylan K, Graff-Radford NR, Dickson DW, Clay-Falcone D, Elman L, McCluskey L, Greene R, Kalb RG, Lee VM, Trojanowski JQ, Ludolph A, Robberecht W, Andersen PM, Nicholson GA, Blair IP, King OD, Bonini NM, Van Deerlin V, Rademakers R, Mourelatos Z, Gitler AD. Couthouis J, et al. Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):20881-90. doi: 10.1073/pnas.1109434108. Epub 2011 Nov 7. Proc Natl Acad Sci U S A. 2011. PMID: 22065782 Free PMC article.

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