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. 2018 Jun 14;9:2347. doi: 10.1038/s41467-018-04796-3

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© The Author(s) 2018

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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Fig. 2 — SpHtp3 is a self-translocating nuclease. a Amino acid sequence of SpHtp3 (top), including the secretion signal (M1-G21, underlined), the RxLR sequence (R48-R51, red) and the predicted nuclease domain (L89-S197, bold). Protein domain structure of SpHtp3 (bottom). b Visualisation of RNA (left, RTG-2 cell RNA) and DNA (right, linearised pET21b) degrading activities of SpHtp3-His₆ and SpHtp3-mRFP (n = 3). c Real-time ribonuclease activity assessment of SpHtp3 wt (black) compared to a negative control (SpHtp1-mRFP, red) and a non-functional mutant of SpHtp3 (GTLG, blue) with RNaseAlert® (n = 2). d Autonomous translocation activity of recombinant SpHtp3-mRFP into living RTG-2 cells at pH 7.5 and 5.5. The control (mRFP only) does not show any translocation. Scale bar: 20 µm (n = 3)