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. 2019 Mar 6;9:3681. doi: 10.1038/s41598-018-38386-6

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Model depicting EloR- and KhpA dependent cell elongation. KhpA binds the KH-II domain of EloR, which recruits KhpA to the division zone where new cell wall is synthesized. At the division zone the EloR/KhpA complex regulates cell elongation by binding RNA. Whether EloR/KhpA binds one or more specific sequence motifs or specific RNA secondary structures, and how binding of RNA regulates cell division are still not settled. A monomeric KhpA does not render cells independent on PBP2b as long as it still forms a complex with EloR. If the interaction between EloR and KhpA is broken, KhpA loses its mid-cell localization and binding to the target RNA(s) is most probably reduced or lost. Since EloR requires the RNA binding activity of KhpA to function, preventing EloR/KhpA complex formation results in compromised cell elongation.