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. 2017 Feb 14;45(8):4915–4928. doi: 10.1093/nar/gkx099

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© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 6. — Yeast two-hybrid and pulldown protein-protein interaction analyses with MORF1 and structure-based mutants. (A) Yeast colony growth of the MORF–MORF protein combinations after 6 days on control medium (SD-TL) and selection medium (SD-TLHA) containing different concentrations of 3AT. The C85S mutant shows interaction similar to the wildtype up to 5 mM 3AT while all other mutants are showing reduced growth at all 3AT concentrations, indicating weaker interaction. (B) Pull-down of GFP tagged MORF1^61-241 and its respective mutants with MBP tagged MORF1 bound to amylose resin (AR) as a bait. Shown are the respective MORF-GFP GFP antibody chemiluminescence signals in the respective gel lanes. Without any protein and with MBP as a bait no GFP antibody signal is detected. The C85S mutant shows a signal similar to the MORF1^61-241 wild type while all other mutated MORFs show reduced signal intensity.