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. 2016 Jun 15;129(12):2407–2415. doi: 10.1242/jcs.184614

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© 2016. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Fig. 5. — eIF4A1 and eIF4A2 are sumoylated on K225 and K226, respectively. (A) Mass spectra of sumoylation products. High-molecular-mass species from an in vitro sumoylation assay were excised from SDS-PAGE gels and analysed by LC-MS/MS. (B) Sequence alignment of human eIF4A1, eIF4A2 and eIF4A3. Sumoylation sites are indicated in red. (C) Position of sumoylation sites on eIF4A1 (i) and eIF4A2 (ii). Pymol-derived figure indicating sumoylation sites on human eIF4A1 (PDB ID 2ZU6) and eIF4A2 (PDB ID 3BOR). ABP, ATP-binding pocket. (D) Schematic indicating organisation of interacting motifs in eIF4G. (E) Positions of sumoylation site (K1386, green) and Q1379 (magenta) in the C-terminal fragment of eIF4G (PDB IB 1UG3).