The AP2 transcription factors DORNROSCHEN and DORNROSCHEN-LIKE redundantly control Arabidopsis embryo patterning via interaction with PHAVOLUTA
The AP2 transcription factors DORNROSCHEN and DORNROSCHEN-LIKE redundantly control Arabidopsis embryo patterning via interaction with PHAVOLUTA
复制标题
DOI：
10.1242/dev.001016
复制
发表时间：
2007-05-01
期刊：
影响因子：
4.6
通讯作者：
Werr, Wolfgang
中科院分区：
文献类型：
--
作者：
Chandler, John W.;Cole, Melanie;Werr, Wolfgang
DORNROSCHEN（DRN）（也称为芽再生增强剂1; ESR 1）和DRN样（DRNL;也称为ESR 2）是编码含AP 2结构域蛋白的两个连锁旁系同源物。DRN突变体显示出胚细胞图案缺陷，并且与DRN 1突变体类似，在不完全脱序时破坏子叶发育。具有弱或强DRN 1等位基因的DRN-DRN 1双突变体显示出更高的外显和极端表型，包括没有子叶的针样胚，证实了两个基因在胚形成中的高度功能冗余。DRN突变体胚胎中PIN 1：：PIN 1-GFP和DR 5：：GFP的表达改变将DRN置于生长素运输和响应的上游。酵母双杂交筛选DRN，然后通过免疫共沉淀和双分子荧光互补揭示PHAVOLUTA（PHV）是一种蛋白质相互作用的伴侣在植物。DRN PHV双突变体显示出胚胎细胞分裂缺陷的增加。DRNL还可以与PHV相互作用，并且DRN和DRNL都可以与III类HD-ZIP家族的其他成员PHABULOSA、REVOLUTA、CORONA和ATHB 8异二聚化。相互作用涉及这些蛋白质的PAS样C-末端区域和DRN/DRNL AP 2结构域。
DORNROSCHEN (DRN) (also known as ENHANCER OF SHOOT REGENERATION1; ESR1) and DRN-LIKE (DRNL; also known as ESR2) are two linked paralogues encoding AP2 domain-containing proteins. drn mutants show embryo cell patterning defects and, similarly to drnl mutants, disrupt cotyledon development at incomplete penetrance. drn drnl double mutants with weak or strong drnl alleles show more highly penetrant and extreme phenotypes, including a pin-like embryo without cotyledons, confirming a high degree of functional redundancy for the two genes in embryo patterning. Altered expression of PIN1:: PIN1-GFP and DR5::GFP in drn mutant embryos places DRN upstream of auxin transport and response. A yeast two-hybrid screen with DRN followed by coimmunoprecipitation and bimolecular fluorescence complementation revealed PHAVOLUTA (PHV) to be a protein interaction partner in planta. drn phv double mutants show an increased penetrance of embryo cell division defects. DRNL can also interact with PHV and both DRN and DRNL can heterodimerise with additional members of the class III HD-ZIP family, PHABULOSA, REVOLUTA, CORONA and ATHB8. Interactions involve the PAS-like C-terminal regions of these proteins and the DRN/DRNL AP2 domain.