Correction to Mutational Replacements at the “Glycine Hinge” of the

Addition/Correction Cite This: Biochemistry 2017, 56, 6626−6626

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Correction to Mutational Replacements at the “Glycine Hinge” of the Escherichia coli Chemoreceptor Tsr Support a Signaling Role for the C‑Helix Residue Andrea Pedetta, Diego Ariel Massazza, María Karina Herrera Seitz, and Claudia Alicia Studdert* Biochemistry 2017, 56 (29), 3850−3862. DOI: 10.1021/acs.biochem.7b00455

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he WebLogo pattern shown in Figure 1B is extracted from a more extended WebLogo pattern for 36H-class chemoreceptors that is shown in Figure S1. However, to show the region as part of the cytoplasmic hairpin, the original alignment had to be inverted, and during this process, involuntary mistakes appeared. The most conspicuous mistake puts a serine residue in a very conserved position, where the correct residue is a methionine. The corrected Figure 1B does now correspond accurately to the alignment in Figure S1.

Figure 1. Architecture and conservation of the “glycine hinge” of the chemoreceptors. (A) Cartoon representation of a Tsr homodimer showing important signaling features. Cylindrical bars represent α-helical regions. Methylation residues are shown as dark gray circles. White circles represent the glycine residues that form the postulated hinge within the coupling subdomain. The inset shows a molecular view of the “glycine hinge” region obtained with PyMol. G340, G341, and G439 residues of the dark gray subunit are colored pink; the other subunit is colored light gray. (B) Conservation analysis of the coupling subdomain in the 36H chemoreceptor class. After retrieving 2428 receptors belonging to the 36H class, we aligned their cytoplasmic domain using the MAFFT engine, and that alignment was used to analyze the amino acid conservation of the coupling subdomain with WebLogo22. This subdomain encompasses N-helix residues 321−362 and C-helix residues 420−461 (E. coli serine receptor Tsr numbering); “glycine hinge” residues are denoted with light blue stars (G340 and G341 in the N-helix and G439 in the C-helix), and knob positions a and d are denoted with red arrowheads.

Received: November 1, 2017 Published: December 4, 2017 © 2017 American Chemical Society

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DOI: 10.1021/acs.biochem.7b01110 Biochemistry 2017, 56, 6626−6626