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. 2020 Mar 10;9(3):669. doi: 10.3390/cells9030669

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Interaction of NBR1 with RPS6. (A) Results of BiFC experiment (the scale bar, 50 µm). The controls are shown in Supplementary Materials Figure S2. (B) Result of Y2H experiment. Full-length NBR1 and NBR1 with C-terminal deletion of 87 amino acids (NBR1ΔUBA), fragments of NBR1 (ZZNBR1) and RPS6B (RPS6W) proteins. (C) Scheme showing the protein fragments involved in the interactions. The RPS6 structure is shown as a model of RS62_ARATH protein from SWISS-MODEL. (D) BiFC experiment demonstrating intracellular localization of RPS6-NBR1 interactions. RPS6A-NBR1 interaction co-localize in some cases with H2B-RFP, used as a nuclear marker. No colocalization with H2B-RFP was not observed in the case of the RPS6B-NBR1 interaction. The co-localized with H2B-RFP BiFC signals are indicated by arrows, not-colocalized by arrowheads.

Interaction of NBR1 with RPS6. (A) Results of BiFC experiment (the scale bar, 50 µm). The controls are shown in Supplementary Materials Figure S2. (B) Result of Y2H experiment. Full-length NBR1 and NBR1 with C-terminal deletion of 87 amino acids (NBR1ΔUBA), fragments of NBR1 (ZZNBR1) and RPS6B (RPS6W) proteins. (C) Scheme showing the protein fragments involved in the interactions. The RPS6 structure is shown as a model of RS62_ARATH protein from SWISS-MODEL. (D) BiFC experiment demonstrating intracellular localization of RPS6-NBR1 interactions. RPS6A-NBR1 interaction co-localize in some cases with H2B-RFP, used as a nuclear marker. No colocalization with H2B-RFP was not observed in the case of the RPS6B-NBR1 interaction. The co-localized with H2B-RFP BiFC signals are indicated by arrows, not-colocalized by arrowheads.