Rice ternary MADS protein complexes containing class B MADS heterodimer.
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.
Seok
Hye-Yeon
HY
Department of Molecular Biology, Pusan National University, Busan 609-735, Republic of Korea.
Park
Hee-Yeon
HY
Park
Ji-Im
JI
Lee
Young-Mi
YM
Lee
Sun-Young
SY
An
Gynheung
G
Moon
Yong-Hwan
YH
D026161:MADS Domain Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012275:Oryza / Q000378:metabolism*; D030821:Plants, Genetically Modified / Q000235:genetics / Q000378:metabolism; D055503:Protein Multimerization; D034622:RNA Interference
D026161:MADS Domain Proteins; D046912:Multiprotein Complexes