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. 2018 Aug 17;8:12411. doi: 10.1038/s41598-018-30015-6

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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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Intramembrane proteolysis of APPTM in solution NMR. (A) Overlaid NMR structures of WT (green) and FAD V44M (orange) APPTM, with residue 44 in stick mode. (B) Structure of PSH (grey) overlaid on presenilin (blue) with an RMSD of 3.1 Å. (C) Intramembrane proteolysis activity of MAMRE50, MCMJR1 and a control intramembrane protease against MBP-APPTM measured by SDS-PAGE after incubation at 37 °C for 12 hrs. Intramembrane proteolysis activity of MCMJR1 (D) and MAMRE50 (E) in solution NMR, evidenced by decreasing APPTM peak intensity and the appearance of sharp peaks in 2D ¹⁵N-¹H HSQC at 40 °C over 24 hours, with enzyme:substrate at 1:1 molar ratio. Similar results were obtained for WT APPTM (data not shown). (F) Determination of the cleavage rate of APPTM from variation of peak intensity over time for select well-resolved peaks with high S/N.