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TAZ
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Du & Poovaiah (2004): A novel CaM-binding protein was isolated through protein-protein interaction based screening of an Arabidopsis cDNA expression library using a 35S calmodulin (CaM) probe. There are four additional homologs in the Arabidopsis genome with similar structures: a BTB domain in the N-terminus and a Zf-TAZ domain in the C-terminus. Hence, they were designated as AtBT1-5 (Arabidopsis thaliana BTB and TAZ domain protein). CaM-binding experiments revealed that all five AtBTs are CaM-binding proteins, and their CaM-binding domains were mapped to the C-terminus. AtBT homologs are also present in rice, but are not present in human, animal, yeast or other organisms, suggesting that the BTB and TAZ domain proteins are plant-specific. The AtBT1-smGFP fusion protein expressed in tobacco BY-2 cells showed that AtBT1 targets the nucleus. Yeast two-hybrid screening using an AtBT1 fragment as bait identified two interacting proteins (AtBET10 and AtBET9) belonging to the family of fsh/Ring3 class transcription regulators. The BTB domain of the AtBTs is required for the interaction, and this protein-protein interaction was confirmed by GST pull-down. AtBET10 also interacts with AtBT2 and AtBT4, and exhibited a transcriptional activation function in yeast cells. AtBTs exhibit varying responses to different stress stimuli, but all five genes responded rapidly to H2O2 and salicylic acid (SA) treatments. These results suggest that AtBTs play a role in transcriptional regulation, and signal molecules such as Ca2+, H2O2, and SA affect transcriptional machinery by altering the expression and conformation of AtBTs which interact with transcriptional activators such as AtBET10.
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Du, L; Poovaiah, BW. 2004. A novel family of Ca2+/calmodulin-binding proteins involved in transcriptional regulation: interaction with fsh/Ring3 class transcription activators. Plant Mol. Biol. 54(4):549-69
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TR
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TFb2
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<a target="_blank" class="awithout" href="https://www.ebi.ac.uk/interpro/entry/IPR004598">InterPro</a> (0): This domain represents the p52/Tfb2 subunit in the TFIIH complex, which is not only required for transcription but also plays a central role in DNA repair.
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Lang, D; Weiche, B; Timmerhaus, G; Richardt, S; Riano-Pachon, DM; Correa, LG; Reski, R; Mueller-Roeber, B; Rensing, SA. 2010. Genome-wide phylogenetic comparative analysis of plant transcriptional regulation: a timeline of loss, gain, expansion, and correlation with complexity. Genome Biol Evol. 2: 488-503
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TR
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tify
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Nishii et al (2000): By differential screening of an arrayed normalized cDNA library from the inflorescence apex in Arabidopsis, a cDNA clone having a deduced amino acid sequence with a motif for a zinc finger was isolated as one of the genes expressed specifically in the reproductive phase. The deduced protein has a modular structure with a putative single C2-C2 zinc-finger motif distantly related to a GATA-1-type finger, a basic region with a sequence resembling a nuclear localization signal, and an acidic region. The gene seemed to have been formed by the exon-shuffling during its molecular evolution, since individual domains are encoded by discrete exons. RNA gel blot analysis showed its expression in shoot apex and flowers in the reproductive phase. The gene was named ZIM for Zinc-finger protein expressed in Inflorescence Meristem. The nuclear localization of ZIM was detected using GFP as a reporter. These results suggest that ZIM is a putative transcription factor involved in inflorescence and flower development.
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Lang, D; Weiche, B; Timmerhaus, G; Richardt, S; Riano-Pachon, DM; Correa, LG; Reski, R; Mueller-Roeber, B; Rensing, SA. 2010. Genome-wide phylogenetic comparative analysis of plant transcriptional regulation: a timeline of loss, gain, expansion, and correlation with complexity. Genome Biol Evol. 2: 488-503,"Nishii, A; Takemura, M; Fujita, H; Shikata, M; Yokota, A; Kohchi, T. 2000. Characterization of a novel gene encoding a putative single zinc-finger protein, ZIM, expressed during the reproductive phase in Arabidopsis thaliana. Biosci. Biotechnol. Biochem. 64(7):1402-9","Vanholme, B; Grunewald, W; Bateman, A; Kohchi, T; Gheysen, G. 2007. The tify family previously known as ZIM. Trends Plant Sci. 12(6):239-44"
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TF
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TRAF
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Stogios et al (2005): The BTB domain (also known as the POZ domain) is a versatile protein-protein interaction motif that participates in a wide range of cellular functions, including transcriptional regulation, cytoskeleton dynamics, ion channel assembly and gating, and targeting proteins for ubiquitination. Several BTB domain structures have been experimentally determined, revealing a highly conserved core structure. The BTB domain is typically found as a single copy in proteins that contain only one or two other types of domain, and this defines the BTB-zinc finger (BTB-ZF), BTB-BACK-kelch (BBK), voltage-gated potassium channel T1 (T1-Kv), MATH-BTB, BTB-NPH3 and BTB-BACK-PHR (BBP) families of proteins, among others. BTB-ZF proteins are also known as the POK (POZ and Krüppel zinc finger) proteins. Many members of this large family have been characterized as important transcriptional factors, and several are implicated in development and cancer, most notably BCL6, leukemia/lymphoma related factor (LRF)/Pokemon, PLZF, hypermethylated in cancer (HIC)1 and Myc interacting zinc finger (MIZ)1.
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Deweindt, C; Albagli, O; Bernardin, F; Dhordain, P; Quief, S; Lantoine, D; Kerckaert, JP; Leprince, D. 1995. The LAZ3/BCL6 oncogene encodes a sequence-specific transcriptional inhibitor: a novel function for the BTB/POZ domain as an autonomous repressing domain. Cell Growth Differ. 6(12):1495-503,"Lang, D; Weiche, B; Timmerhaus, G; Richardt, S; Riano-Pachon, DM; Correa, LG; Reski, R; Mueller-Roeber, B; Rensing, SA. 2010. Genome-wide phylogenetic comparative analysis of plant transcriptional regulation: a timeline of loss, gain, expansion, and correlation with complexity. Genome Biol Evol. 2: 488-503","Stogios, PJ; Downs, GS; Jauhal, JJ; Nandra, SK; Privé, GG. 2005. Sequence and structural analysis of BTB domain proteins. Genome Biol. 6(10):R82"
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TR
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Trihelix
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Kaplan-Levy et al (2012): GT factors are the founding members of the trihelix transcription factor family. Genomic studies have revealed 30 members of this family in Arabidopsis and 31 in rice, falling into five clades. Newly discovered functions involve responses to salt and pathogen stresses, the development of perianth organs, trichomes, stomata and the seed abscission layer, and the regulation of late embryogenesis.
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Kaplan-Levy, RN; Brewer, PB; Quon, T; Smyth, DR. 2012. The trihelix family of transcription factors--light, stress and development. Trends Plant Sci. 17(3):163-71,"Nagano, Y. 2000. Several features of the GT-factor trihelix domain resemble those of the Myb DNA-binding domain. Plant Physiol. 124(2):491-4","Nagano, Y; Inaba, T; Furuhashi, H; Sasaki, Y. 2001. Trihelix DNA-binding protein with specificities for two distinct cis-elements: both important for light down-regulated and dark-inducible gene expression in higher plants. J. Biol. Chem. 276(25):22238-43","Smalle, J; Kurepa, J; Haegman, M; Gielen, J; Van Montagu, M; Van Der Straeten, D. 1998. The trihelix DNA-binding motif in higher plants is not restricted to the transcription factors GT-1 and GT-2. Proc. Natl. Acad. Sci. U.S.A. 95(6):3318-22","Zhou, DX. 1999. Regulatory mechanism of plant gene transcription by GT-elements and GT-factors. Trends Plant Sci 4(6):210-214","Kaplan-Levy, RN; Brewer, PB; Quon, T; Smyth, DR. 2012. The trihelix family of transcription factors--light, stress and development. Trends Plant Sci. 17(3):163-71","Nagano, Y. 2000. Several features of the GT-factor trihelix domain resemble those of the Myb DNA-binding domain. Plant Physiol. 124(2):491-4","Nagano, Y; Inaba, T; Furuhashi, H; Sasaki, Y. 2001. Trihelix DNA-binding protein with specificities for two distinct cis-elements: both important for light down-regulated and dark-inducible gene expression in higher plants. J. Biol. Chem. 276(25):22238-43","Smalle, J; Kurepa, J; Haegman, M; Gielen, J; Van Montagu, M; Van Der Straeten, D. 1998. The trihelix DNA-binding motif in higher plants is not restricted to the transcription factors GT-1 and GT-2. Proc. Natl. Acad. Sci. U.S.A. 95(6):3318-22","Zhou, DX. 1999. Regulatory mechanism of plant gene transcription by GT-elements and GT-factors. Trends Plant Sci 4(6):210-214"
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TF
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TUB
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Lai et al (2004): In mammals, TUBBY-like proteins play an important role in maintenance and function of neuronal cells during postdifferentiation and development. We have identified a TUBBY-like protein gene family with 11 members in Arabidopsis, named AtTLP1-11. Although seven of the AtTLP genes are located on chromosome I, no local tandem repeats or gene clusters are identified. Except for AtTLP4, reverse transcription-PCR analysis indicates that all these genes are expressed in various organs in 6-week-old Arabidopsis. AtTLP1, 2, 3, 6, 7, 9, 10, and 11 are expressed ubiquitously in all the organs tested, but the expression of AtTLP5 and 8 shows dramatic organ specificity. These 11 family members share 30% to 80% amino acid similarities across their conserved C-terminal tubby domains. Unlike the highly diverse N-terminal region of animal TUBBY-like proteins, all AtTLP members except AtTLP8 contain a conserved F-box domain (51-57 residues). The interaction between AtTLP9 and ASK1 (Arabidopsis Skp1-like 1) is confirmed via yeast (Saccharomyces cerevisiae) two-hybrid assays. Abscisic acid (ABA)-insensitive phenotypes are observed for two independent AtTLP9 mutant lines, whereas transgenic plants overexpressing AtTLP9 are hypersensitive to ABA. These results suggest that AtTLP9 may participate in the ABA signaling pathway.
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Boggon, TJ; Shan, WS; Santagata, S; Myers, SC; Shapiro, L. 1999. Implication of tubby proteins as transcription factors by structure-based functional analysis. Science 286(5447):2119-25,"Lai, CP; Lee, CL; Chen, PH; Wu, SH; Yang, CC; Shaw, JF. 2004. Molecular analyses of the Arabidopsis TUBBY-like protein gene family. Plant Physiol. 134(4):1586-97","Santagata, S; Boggon, TJ; Baird, CL; Gomez, CA; Zhao, J; Shan, WS; Myszka, DG; Shapiro, L. 2001. G-protein signaling through tubby proteins. Science 292(5524):2041-50"
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TF
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ULT
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Carles et al (2005): The higher-plant shoot apical meristem is a dynamic structure continuously producing cells that become incorporated into new leaves, stems and flowers. The maintenance of a constant flow of cells through the meristem depends on coordination of two antagonistic processes: self-renewal of the stem cell population and initiation of the lateral organs. This coordination is stringently controlled by gene networks that contain both positive and negative components. We have previously defined the ULTRAPETALA1 (ULT1) gene as a key negative regulator of cell accumulation in Arabidopsis shoot and floral meristems, because mutations in ULT1 cause the enlargement of inflorescence and floral meristems, the production of supernumerary flowers and floral organs, and a delay in floral meristem termination. Here, we show that ULT1 negatively regulates the size of the WUSCHEL (WUS)-expressing organizing center in inflorescence meristems. We have cloned the ULT1 gene and find that it encodes a small protein containing a B-box-like motif and a SAND domain, a DNA-binding motif previously reported only in animal transcription factors. ULT1 and its Arabidopsis paralog ULT2 define a novel small gene family in plants. ULT1 and ULT2 are expressed coordinately in embryonic shoot apical meristems, in inflorescence and floral meristems, and in developing stamens, carpels and ovules. Additionally, ULT1 is expressed in vegetative meristems and leaf primordia. ULT2 protein can compensate for mutant ULT1 protein when overexpressed in an ult1 background, indicating that the two genes may regulate a common set of targets during plant development. Downregulation of both ULT genes can lead to shoot apical meristem arrest shortly after germination, revealing a requirement for ULT activity in early development.
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Carles, CC; Choffnes-Inada, D; Reville, K; Lertpiriyapong, K; Fletcher, JC. 2005. ULTRAPETALA1 encodes a SAND domain putative transcriptional regulator that controls shoot and floral meristem activity in Arabidopsis. Development 132(5):897-911
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TF
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VARL
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Duncan et al (2007): Chlamydomonas reinhardtii, Volvox carteri, and their relatives in the family Volvocaceae provide an excellent opportunity for studying how multicellular organisms with differentiated cell types evolved from unicellular ancestors. While C. reinhardtii is unicellular, V. carteri is multicellular with two cell types, one of which resembles C. reinhardtii cytologically but is terminally differentiated. Maintenance of this "somatic cell" fate is controlled by RegA, a putative transcription factor. We recently showed that RegA shares a conserved region with several predicted V. carteri and C. reinhardtii proteins and that this region, the VARL domain, is likely to include a DNA-binding SAND domain. As the next step toward understanding the evolutionary origins of the regA gene, we analyzed the genome sequences of C. reinhardtii and V. carteri to identify additional genes with the potential to encode VARL domain proteins. Here we report that the VARL gene family, which consists of 12 members in C. reinhardtii and 14 in V. carteri, has experienced a complex evolutionary history in which members of the family have been both gained and lost over time, although several pairs of potentially orthologous genes can still be identified. We find that regA is part of a tandem array of four VARL genes in V. carteri but that a similar array is absent in C. reinhardtii. Most importantly, our phylogenetic analysis suggests that a proto-regA gene was present in a common unicellular ancestor of V. carteri and C. reinhardtii and that this gene was lost in the latter lineage.
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Duncan, L; Nishii, I; Harryman, A; Buckley, S; Howard, A; Friedman, NR; Miller, SM. 2007. The VARL gene family and the evolutionary origins of the master cell-type regulatory gene, regA, in Volvox carteri. J. Mol. Evol. 65(1):1-11
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TF
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VOZ
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Mitsuda et al (2004): A 38-bp pollen-specific cis-acting region of the AVP1 gene is involved in the expression of the Arabidopsis thaliana V-PPase during pollen development. Here, we report the isolation and structural characterization of AtVOZ1 and AtVOZ2, novel transcription factors that bind to the 38-bp cis-acting region of A. thaliana V-PPase gene, AVP1. AtVOZ1 and AtVOZ2 show 53% amino acid sequence similarity. Homologs of AtVOZ1 and AtVOZ2 are found in various vascular plants as well as a moss, Physcomitrella patens. Promoter-beta-glucuronidase reporter analysis shows that AtVOZ1 is specifically expressed in the phloem tissue and AtVOZ2 is strongly expressed in the root. In vivo transient effector-reporter analysis in A. thaliana suspension-cultured cells demonstrates that AtVOZ1 and AtVOZ2 function as transcriptional activators in the Arabidopsis cell. Two conserved regions termed Domain-A and Domain-B were identified from an alignment of AtVOZ proteins and their homologs of O. sativa and P. patens. AtVOZ2 binds as a dimer to the specific palindromic sequence, GCGTNx7ACGC, with Domain-B, which is comprised of a functional novel zinc coordinating motif and a conserved basic region. Domain-B is shown to function as both the DNA-binding and the dimerization domains of AtVOZ2. From highly the conservative nature among all identified VOZ proteins, we conclude that Domain-B is responsible for the DNA binding and dimerization of all VOZ-family proteins and designate it as the VOZ-domain.
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Mitsuda, N; Hisabori, T; Takeyasu, K; Sato, MH. 2004. VOZ; isolation and characterization of novel vascular plant transcription factors with a one-zinc finger from Arabidopsis thaliana. Plant Cell Physiol. 45(7):845-54
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TF
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Whirly
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Desveaux et al (2002): The single-stranded DNA (ssDNA) binding subunit of the plant transcription factor p24 is representative of a novel family of ubiquitous plant-specific proteins that we refer to as the Whirly family because of their quaternary structure.
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Lang, D; Weiche, B; Timmerhaus, G; Richardt, S; Riano-Pachon, DM; Correa, LG; Reski, R; Mueller-Roeber, B; Rensing, SA. 2010. Genome-wide phylogenetic comparative analysis of plant transcriptional regulation: a timeline of loss, gain, expansion, and correlation with complexity. Genome Biol Evol. 2: 488-503,"Desveaux, D; Allard, J; Brisson, N; Sygusch, J. 2002. A new family of plant transcription factors displays a novel ssDNA-binding surface. Nat Struct Biol. 9(7):512-7"
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TF
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WRKY
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Wu et al (2005): WRKY transcription factors, originally isolated from plants contain one or two conserved WRKY domains, about 60 amino acid residues with the WRKYGQK sequence followed by a C2H2 or C2HC zinc finger motif. Evidence is accumulating to suggest that the WRKY proteins play significant roles in responses to biotic and abiotic stresses, and in development. In this research, we identified 102 putative WRKY genes from the rice genome and compared them with those from Arabidopsis. The WRKY genes from rice and Arabidopsis were divided into three groups with several subgroups on the basis of phylogenies and the basic structure of the WRKY domains (WDs). The phylogenetic trees generated from the WDs and the genes indicate that the WRKY gene family arose during evolution through duplication and that the dramatic amplification of rice WRKY genes in group III is due to tandem and segmental gene duplication compared with those of Arabidopsis. The result suggests that some of the rice WRKY genes in group III are evolutionarily more active than those in Arabidopsis, and may have specific roles in monocotyledonous plants. Further, it was possible to identify the presence of WRKY-like genes in protists (Giardia lamblia and Dictyostelium discoideum) and green algae Chlamydomonas reinhardtii through database research, demonstrating the ancient origin of the gene family. The results obtained by alignments of the WDs from different species and other analysis imply that domain gain and loss is a divergent force for expansion of the WRKY gene family, and that a rapid amplification of the WRKY genes predate the divergence of monocots and dicots. On the basis of these results, we believe that genes encoding a single WD may have been derived from the C-terminal WD of the genes harboring two WDs. The conserved intron splicing positions in the WDs of higher plants offer clues about WRKY gene evolution, annotation, and classification.
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Eulgem, T; Rushton, PJ; Robatzek, S; Somssich, IE. 2000. The WRKY superfamily of plant transcription factors. Trends Plant Sci. 5(5):199-206,"Ulker, B; Somssich, IE. 2004. WRKY transcription factors: from DNA binding towards biological function. Curr. Opin. Plant Biol. 7(5):491-8","Wu, KL; Guo, ZJ; Wang, HH; Li, J. 2005. The WRKY family of transcription factors in rice and Arabidopsis and their origins. DNA Res. 12(1):9-26","Zhang, Y; Wang, L. 2005. The WRKY transcription factor superfamily: its origin in eukaryotes and expansion in plants. BMC Evol. Biol. 5(1):1"
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TF
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Zinc finger, AN1 and A20 type
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<a target="_blank" class="awithout" href="http://pfam.xfam.org/family/PF01428">PFAM</a> (0): The AN1-type zinc finger domain has a dimetal (zinc)-bound alpha/beta fold. Certain stress-associated proteins contain the AN1 domain, often in combination with A20 zinc finger domains or C2H2 domains.
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Lang, D; Weiche, B; Timmerhaus, G; Richardt, S; Riano-Pachon, DM; Correa, LG; Reski, R; Mueller-Roeber, B; Rensing, SA. 2010. Genome-wide phylogenetic comparative analysis of plant transcriptional regulation: a timeline of loss, gain, expansion, and correlation with complexity. Genome Biol Evol. 2: 488-503,"Vij, S; Tyagi, AK. 2006. Genome-wide analysis of the stress associated protein (SAP) gene family containing A20/AN1 zinc-finger(s) in rice and their phylogenetic relationship with Arabidopsis. Mol Genet Genomics 276(6):565-75"
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TR
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Zinc finger, MIZ type
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<a target="_blank" class="awithout" href="http://pfam.xfam.org/family/PF02891">PFAM</a> (0): The MIZ-type zinc finger domain is a sequence specific DNA binding domain that is part of proteins like Miz1 that can function as a positive-acting transcription factor. The name MIZ is derived from Msx-interacting-zinc finger.
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Lang, D; Weiche, B; Timmerhaus, G; Richardt, S; Riano-Pachon, DM; Correa, LG; Reski, R; Mueller-Roeber, B; Rensing, SA. 2010. Genome-wide phylogenetic comparative analysis of plant transcriptional regulation: a timeline of loss, gain, expansion, and correlation with complexity. Genome Biol Evol. 2: 488-503
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TF
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Zinc finger, ZPR1
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<a target="_blank" class="awithout" href="http://pfam.xfam.org/family/PF03367">PFAM</a> (0): The zinc-finger protein ZPR1 is localised to the cytoplasm in quiescent cells; in proliferating cells treated with EGF or with other mitogens it accumulates in the nucleolus. Upon stimulation by EGF, ZPR1 directly binds the eukaryotic translation elongation factor-1alpha (eEF-1alpha) to form ZPR1/eEF-1alpha complexes. These move into the nucleus, localising particularly at the nucleolus. ZPR1 is thought to be involved in pre-ribosomal RNA expression. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion.
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Lang, D; Weiche, B; Timmerhaus, G; Richardt, S; Riano-Pachon, DM; Correa, LG; Reski, R; Mueller-Roeber, B; Rensing, SA. 2010. Genome-wide phylogenetic comparative analysis of plant transcriptional regulation: a timeline of loss, gain, expansion, and correlation with complexity. Genome Biol Evol. 2: 488-503,"Gangwani, L1; Mikrut, M; Galcheva-Gargova, Z; Davis, RJ. 1998. Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells. J Cell Biol 143(6):1471-84","Galcheva-Gargova, Z; Gangwani, L; Konstantinov, KN; Mikrut, M; Theroux, SJ; Enoch, T; Davis RJ. 1998. The cytoplasmic zinc finger protein ZPR1 accumulates in the nucleolus of proliferating cells. Mol Biol Cell 9(10):2963-71"
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TR
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Zn_clus
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Pan & Coleman (1990): The DNA-binding domain of the transcription factor GAL4, consisting of the 62 N-terminal residues and denoted GAL4(62*), contains a Cys-Xaa2-Cys-Xaa6-Cys-Xaa6-Cys-Xaa2-Cys-Xaa6+ ++-Cys motif, which has been shown previously to bind two Zn(II) or Cd(II) ions. Binding of Zn(II) or Cd(II) is essential for the recognition by GAL4 of the specific palindromic DNA sequence to which it binds upstream of genes for galactose-metabolizing enzymes, the UASG sequence. On the basis of the 113Cd NMR chemical shifts of the two bound 113Cd(II) ions, we propose a binuclear cluster model for this Zn(II)-binding subdomain. 1H-113Cd heteronuclear multiple-quantum NMR spectroscopy and phase-sensitive double-quantum filtered 1H correlation spectroscopy of the 112Cd(II)- and 113Cd(II)-substituted GAL4(62*) derivatives provide direct evidence that the two bound 113Cd(II) ions are coordinated only by the six cysteine residues, two of which form bridging ligands between the two 113Cd(II) ions. The latter can be identified from the pattern of 1H-113Cd J coupling. Thus a binuclear metal ion cluster rather than a "zinc finger" is formed by the six cysteine residues of the GAL4 DNA-binding domain. This model can be directly applied to eight other fungal transcription factors which have been shown to contain similarly spaced Cys6 clusters. 1H NMR spectra of apo-GAL4(62*) suggest conformational fluctuation of the metal-binding subdomain upon removal of Zn(II) or Cd(II). Both Cd(II)2- and Zn(II)2-containing species of GAL4 can be formed, and the similar 1H NMR spectra suggest similar conformations.
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Pan, T; Coleman, JE. 1990. GAL4 transcription factor is not a zinc finger" but forms a Zn(II)2Cys6 binuclear cluster. Proc. Natl. Acad. Sci. U.S.A. 87(6):2077-81"
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TF
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ZPR
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ZPR proteins are a group of transcriptional regulators that were derived by a duplication event of a C3HDZ protein in the common ancestor of ferns and seed plants and subsequent degenerative mutations. They are involved in the regulation of C3HDZ and in the regulation of plant form and growth (Floyd et al., 2014). Furthermore, ZPR regulators display the important role of gene duplications in the complexity of land plant developmental complexity (Floyd et al., 2014).
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Floyd, S. K., Ryan, J. G., Conway, S. J., Brenner, E., Burris, K. P., Burris, J. N., Chen, T., Edger, P. P., Graham, S. W., Leebens-Mack, J. H., Pires, J. C., Rothfels, C. J., Sigel, E. M., Stevenson, D. W., Neal Stewart, C., Wong, G. K.-S., & Bowman, J. L. (2014). Origin of a novel regulatory module by duplication and degeneration of an ancient plant transcription factor. Molecular Phylogenetics and Evolution, 81, 159–173. https://doi.org/10.1016/j.ympev.2014.06.017
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TR
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