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.1997 Jun 24;94(13):7076-81.
doi: 10.1073/pnas.94.13.7076.

The AP2 domain of APETALA2 defines a large new family of DNA binding proteins in Arabidopsis

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The AP2 domain of APETALA2 defines a large new family of DNA binding proteins in Arabidopsis

J K Okamuro et al. Proc Natl Acad Sci U S A..

Abstract

APETALA2 (AP2) plays an important role in the control of Arabidopsis flower and seed development and encodes a putative transcription factor that is distinguished by a novel DNA binding motif referred to as the AP2 domain. In this study we show that the AP2 domain containing or RAP2 (related to AP2) family of proteins is encoded by a minimum of 12 genes in Arabidopsis. The RAP2 genes encode two classes of proteins, AP2-like and EREBP-like, that are defined by the number of AP2 domains in each polypeptide as well as by two sequence motifs referred to as the YRG and RAYD elements that are located within each AP2 domain. RAP2 genes are differentially expressed in flower, leaf, inflorescence stem, and root. Moreover, the expression of at least three RAP2 genes in vegetative tissues are controlled by AP2. Thus, unlike other floral homeotic genes, AP2 is active during both reproductive and vegetative development.

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Figures

Figure 1
Figure 1
AP2 domain sequence and structure.Arabidopsis RAP2 amino acid sequences were determined and compared as described. Gene names are shown to the left of each sequence. The number of amino acid residues within each AP2 domain is shown to the right. Sequence gaps were introduced to maximize sequence alignments. The position of amino acid residues and sequence gaps within the AP2 domain alignments are numbered 1–77 for reference. The location of the conserved YRG and RAYD elements are indicated by brackets. Shaded boxes highlight regions of sequence similarity. Positively charged amino acids within the YRG element are indicated by + signs above the residues. The location of the 18-amino acid core region that is predicted to form an amphipathic α-helix in AP2 (9) is indicated by a bracket. Residues within the RAYD element of each AP2 domain that are predicted to form an amphipathic α-helix are underlined. (A) AP2-like AP2 domains. Amino acid sequence alignment between the AP2 domain repeats R1 and R2 contained within AP2 (9), ANT (14, 15), and RAP2.7 is shown. Brackets above the sequences designate the conserved YRG and RAYD blocks described above. The filled circle and asterisk indicate the positions of theap2-1, andap2-5 mutations, respectively (9). Amino acid residues that constitute a consensus AP2 domain motif for AP2, ANT, and RAP2.7 is shown below the alignment with invariant residues shown capitalized. The GenBank accession number forAP2 is U12546. (B) EREBP-like AP2 domains. Amino acid sequence alignment between the AP2 domains contained within the tobacco EREBPs and theArabidopsis EREBP-like RAP2 proteins is shown. GenBank accession numbers for EREBP-1, EREBP-2, EREBP-3, and EREBP-4 are D38123, D38126, D38124, and D38125, respectively. (C) Schematic diagrams of the putative RAP2.7-R1, AP2-R1, and ANT-R1 amphipathic α-helices. Amino acid residues within the RAP2.7-R1, AP2-R1, and ANT-R1 motifs shown underlined inA that are predicted to form amphipathic α-helices are schematically displayed with residues rotating clockwise by 100° per residue to form helical structures. Arrows directed toward or away from the center of the helical wheel diagrams indicate the negative or positive degree of hydrophobicity as defined by Joneset al. (33). Positively and negatively charged amino acid residues are designated by + and − signs, respectively. (D) Schematic diagrams of the putative RAP2.2, RAP2.5, RAP2-12, and EREBP-3 amphipathic α-helices. Amino acid residues within the RAP2.2, RAP2.5, RAP2-12, and EREBP-3 motifs shown underlined inB that are predicted to form amphipathic α-helices are schematically displayed as described inC. (E) Sequence alignment between the 25–26 amino acid linker regions in AP2, ANT, and RAP2.7. R1 and R2 designate the positions of the R1 and R2 repeats within AP2, ANT, and RAP2.7 relative to the linker region sequences. Boxes designate invariant residues within the conserved linker regions. Amino acid residues that constitute a consensus linker region motif for AP2, ANT, and RAP2.7 are shown below the alignment with invariant residues shown capitalized. The arrowhead indicates the position of theant-3 mutation described by Klucheret al. (15).
Figure 2
Figure 2
RAP2 gene expression inArabidopsis. Wild-type (WT) andap2-10 mutant (M) flower (F), leaf (L), stem (S), and root (R) polysomal poly(A) mRNAs were fractionated on denaturing agarose gels, transferred to nylon membranes, and reacted with labeledAP2, RAP2.1, RAP2.2, RAP2.3, andRAP2.4 gene-specific DNA probes as outlined inMaterials and Methods. Flower mRNAs were isolated from inflorescences containing stages 1–10 floral buds (34). Leaf, stem, and root mRNAs were isolated from young expanding rosette leaves, inflorescence stem internode tissue, and hydroponically grown root tissue, respectively. mRNA sizes are shown to the right. Lanes F, L, S, and R contain 4 μg of mRNA. (A)AP2 gene expression in wild-typeArabidopsis. (B)RAP2.1 gene expression in wild-type L-er plants. (C)RAP2.2 gene expression in wild-type L-er andap2-10 mutant plants. (D)RAP2.3 gene expression in wild-type L-er andap2-10 mutant plants. (E)RAP2.4 gene expression in wild-type L-er andap2-10 mutant plants. (F)RAP2 gene expression in wild-type C24 andap2-10 mutant stems. LabeledRAP2.2, RAP2.3, andRAP2.4 gene-specific DNA fragments were hybridized to gel blots containing inflorescence stem mRNA from wild-type and mutant plants. Lanes WT and M contain 4 μg of mRNA.
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