Rice ternary MADS protein complexes containing class B MADS heterodimer

Biochem Biophys Res Commun. 2010 Oct 29;401(4):598-604. doi: 10.1016/j.bbrc.2010.09.108. Epub 2010 Oct 1.

Abstract

To investigate ternary MADS protein complexes involved in the regulation of floral organ development in rice, we identified MADS proteins interacting with the class B MADS heterodimers, OsMADS16-OsMADS4 and OsMADS16-OsMADS2, using yeast three-hybrid assay. The class B heterodimers interacted with OsMADS6, 7, 8, 14 and 17, which belong to AP1-like, SEP-like or AGL6-like MADS proteins, generating ternary complexes. The entire region of the K and C domains of OsMADS4 was required for the formation of the OsMADS16-OsMADS4-OsMADS6 and OsMADS16-OsMADS4-OsMADS7 ternary complexes. Analysis results of transgenic plants concomitantly suppressing OsMADS4 and OsMADS6, together with the results of previous studies, suggest that the OsMADS16-OsMADS4-OsMADS6 ternary complex plays an important role in floral development, especially lodicule development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • MADS Domain Proteins / chemistry
  • MADS Domain Proteins / genetics
  • MADS Domain Proteins / metabolism*
  • Multiprotein Complexes / chemistry
  • Multiprotein Complexes / genetics
  • Multiprotein Complexes / metabolism*
  • Oryza / metabolism*
  • Plants, Genetically Modified / genetics
  • Plants, Genetically Modified / metabolism
  • Protein Multimerization
  • RNA Interference

Substances

  • MADS Domain Proteins
  • Multiprotein Complexes