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SVP-like MADS-box protein from Carya cathayensis forms higher-order complexes.

Authors
  • Wang, Jingjing
  • Hou, Chuanming
  • Huang, Jianqin
  • Wang, Zhengjia
  • Xu, Yingwu
Type
Published Article
Journal
Plant Physiology and Biochemistry
Publisher
Elsevier
Publication Date
Mar 01, 2015
Volume
88
Pages
9–16
Identifiers
DOI: 10.1016/j.plaphy.2015.01.002
PMID: 25602439
Source
Medline
Keywords
License
Unknown

Abstract

To properly regulate plant flowering time and construct floral pattern, MADS-domain containing transcription factors must form multimers including homo- and hetero-dimers. They are also active in forming hetero-higher-order complexes with three to five different molecules. However, it is not well known if a MADS-box protein can also form homo-higher-order complex. In this study a biochemical approach is utilized to provide insight into the complex formation for an SVP-like MADS-box protein cloned from hickory. The results indicated that the protein is a heterogeneous higher-order complex with the peak population containing over 20 monomers. Y2H verified the protein to form homo-complex in yeast cells. Western blot of the hickory floral bud sample revealed that the protein exists in higher-order polymers in native. Deletion assays indicated that the flexible C-terminal residues are mainly responsible for the higher-order polymer formation and the heterogeneity. Current results provide direct biochemical evidences for an active MADS-box protein to be a high order complex, much higher than a quartermeric polymer. Analysis suggests that a MADS-box subset may be able to self-assemble into large complexes, and thereby differentiate one subfamily from the other in a higher-order structural manner. Present result is a valuable supplement to the action of mechanism for MADS-box proteins in plant development.

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