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. 2013 Aug 9;8(8):e71856. doi: 10.1371/journal.pone.0071856

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© 2013 Tripathi, Obermann

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Purified Hsp90α, Hsp103, Hop, Aha 1 and Cdc37 were mixed as indicated and fractionated by gel filtration chromatography on a Superdex 200 column. Fractions were analyzed by SDS-PAGE. Marker proteins are shown on top (thyroglobulin, 669 kDa; BSA, 67 kDa). The shift of the cochaperones Hop, Aha1 and Cdc37 indicating complex formation with Hsp90α and Hsp103 is marked by red, blue or green dashed lines, respectively. For the Hsp103+Aha1 and Hsp103+Cdc37 interaction runs the cochaperones were blotted with specific antibodies to prove the identity of the shifted Aha1 and Cdc37 bands that indicate complex formation with Hsp103.