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ATHB17Δ113 forms homodimers and makes heterodimers with maize HD-Zip II proteins.

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posted on 15.04.2014, 04:30 by Elena A. Rice, Abha Khandelwal, Robert A. Creelman, Cara Griffith, Jeffrey E. Ahrens, J. Philip Taylor, Lesley R. Murphy, Siva Manjunath, Rebecca L. Thompson, Matthew J. Lingard, Stephanie L. Back, Huachun Larue, Bonnie R. Brayton, Amanda J. Burek, Shiv Tiwari, Luc Adam, James A. Morrell, Rico A. Caldo, Qing Huai, Jean-Louis K. Kouadio, Rosemarie Kuehn, Anagha M. Sant, William J. Wingbermuehle, Rodrigo Sala, Matt Foster, Josh D. Kinser, Radha Mohanty, Dongming Jiang, Todd E. Ziegler, Mingya G. Huang, Saritha V. Kuriakose, Kyle Skottke, Peter P. Repetti, T. Lynne Reuber, Thomas G. Ruff, Marie E. Petracek, Paul J. Loida

Maize leaf protoplasts were (A) mock- transformed or transformed with constructs expressing CFP, MYC::HA and CFP tagged ATHB17Δ113 alone or CFP and ATHB17Δ113::CFP in combination with ATHB17Δ113::MYC construct, (B) transformed (filled bars) with constructs expressing CFP or each of the CFP tagged HD-Zip IIs alone or co-transformed (empty bars) with the construct expressing ATHB17Δ113::MYC-HA. Cellular extracts were co-immunoprecipitated using anti-MYC antibody and the immunoprecipitated complex was probed with anti-CFP antibody and visualized using phycoerythrin-conjugated reporter molecules. One HD-Zip I, Zmhdz3, was used to evaluate interaction with ATHB17Δ113. Nomenclature of HD-Zip II and HD-Zip I constructs is based on Zhao et al.[22].

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