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. 2017 May 1;31(9):927–938. doi: 10.1101/gad.297580.117

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© 2017 Lin et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 4. — Recognition mechanism of EPF1 by ERL1^LRR–TMM^LRR. (A) Overall structure of the EPF1–ERL1^LRR–TMM^LRR complex. (N) N terminus; (C) C terminus. Color codes are indicated. (B) Detailed interactions of the N-terminal side of EPF1 with ERL1^LRR–TMM^LRR. (C) Detailed interactions of the central region of EPF1 with ERL1^LRR–TMM^LRR. (D) Detailed interactions of EPF1 with ERL1^LRR–TMM^LRR. (E) Mutagenesis analysis of EPF1-6xHis's interaction with ERL1^LRR–TMM^LRR in vitro. The pull-down assays were performed as described in Figure 3A. (F) Effects of the mutations of EPF1 on the stomatal density of Arabidopsis cotyledons; the concentration of peptide was 10 µM. The error bars show SD. n > 8. (*) P < 0.05; (**) P < 0.01, versus the controls by Student's t-test.