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. Author manuscript; available in PMC: 2016 Sep 27.
Published in final edited form as: J Mol Biol. 2016 Feb 6;428(6):1180–1196. doi: 10.1016/j.jmb.2016.01.031

Fig. 5. Binding of Lsm11 and NPAT to the C-terminal region of FLASH is mutually-exclusive.

Fig. 5

A. BLASTP-generated amino acid sequence alignment of the C-terminal regions of human FLASH and YARP. Non-identical amino acids that are unlikely to affect the overall structure of each protein are indicated with the plus sign. α-helices are underlined. B. GST-tagged proteins indicated at the top of each lane were incubated with 35S-labeled Lsm11 169N (top panels) or NPAT 131C (bottom panels) and their binding analyzed by the GST pull down assay. Proteins were collected on glutathione beads, separated on a SDS/polyacrylamide gel and detected by either staining with Coomassie blue (GST proteins, bottom panels) or by autoradiography (35S-labeled proteins, top panels). C. Binding of GST-tagged YARP 97C and FLASH 60C, either alone (lanes 2 and 4) or pre-bound to NPAT 69C (lanes 3 and 5), to 35S-labeled Lsm11 169N.