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. 2012 Feb 17;7(2):e30846. doi: 10.1371/journal.pone.0030846

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Alinsug et al.

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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A. HDA5 exhibited positive interaction with 14-3-3 K and ε in the cytoplasm indicating that HDA5 requires these chaperones for its nuclear export and cytoplasmic retention considering that it does not contain any nuclear export signal within its amino acid sequence. B. On the contrary, HDA15 did not elicit any interaction with 14-3-3 K nor ε suggesting that it may rely on its own nuclear localization and export signals. C. CoIP results further confirm the positive association of HDA5 with 14-3-3 K and ε. HDA5-GFP was co-transfected into protoplasts with myc-tagged 14-3-3 K or 14-3-3 ε. HDA5 was detected using anti-GFP while 14-3-3 proteins were immunoprecipitated with anti-myc monoclonal antibody. Asterisk and arrowheads indicate non-specific bands and 14-3-3-myc, respectively.