Determination of the Motif Responsible for Interaction between the Rice APETALA1/AGAMOUS-LIKE9 Family Proteins Using a Yeast Two-Hybrid System1

DOI PDF 被引用文献7件
  • Yong-Hwan Moon
    Department of Life Science, Pohang University of Science and Technology, Pohang 790–784, Republic of Korea
  • Hong-Gyu Kang
    Department of Life Science, Pohang University of Science and Technology, Pohang 790–784, Republic of Korea
  • Ji-Young Jung
    Department of Life Science, Pohang University of Science and Technology, Pohang 790–784, Republic of Korea
  • Jong-Seong Jeon
    Department of Life Science, Pohang University of Science and Technology, Pohang 790–784, Republic of Korea
  • Soon-Kee Sung
    Department of Life Science, Pohang University of Science and Technology, Pohang 790–784, Republic of Korea
  • Gynheung An
    Department of Life Science, Pohang University of Science and Technology, Pohang 790–784, Republic of Korea

抄録

<jats:title>Abstract</jats:title><jats:p>A MADS family gene,OsMADS6, was isolated from a rice (Oryza sativa L.) young flower cDNA library usingOsAMDS1 as a probe. With this clone, various MADS box genes that encode for protein-to-protein interaction partners of the OsMADS6 protein were isolated by the yeast two-hybrid screening method. On the basis of sequence homology, OsMADS6 and the selected partners can be classified in theAPETALA1/AGAMOUS-LIKE9 (AP1/AGL9) family. One of the interaction partners,OsMADS14, was selected for further study. Both genes began expression at early stages of flower development, and their expression was extended into the later stages. In mature flowers theOsMADS6 transcript was detectable in lodicules and also weakly in sterile lemmas and carpels, whereas theOsMADS14 transcript was detectable in sterile lemmas, paleas/lemmas, stamens, and carpels. Using the yeast two-hybrid system, we demonstrated that the region containing of the 109th to 137th amino acid residues of OsMADS6 is indispensable in the interaction with OsMADS14. Site-directed mutation analysis revealed that the four periodical leucine residues within the region are essential for this interaction. Furthermore, it was shown that the 14 amino acid residues located immediately downstream of the K domain enhance the interaction, and that the two leucine residues within this region play an important role in that enhancement.</jats:p>

収録刊行物

  • Plant Physiology

    Plant Physiology 120 (4), 1193-1204, 1999-08-01

    Oxford University Press (OUP)

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