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Rcd1-like
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Okazaki et al (1998): In the fission yeast Schizosaccharomyces pombe, the onset of sexual development is controlled mainly by two external signals, nutrient starvation and mating pheromone availability. We have isolated a novel gene named rcd1+ as a key factor required for nitrogen starvation-induced sexual development. rcd1+ encodes a 283-amino-acid protein with no particular motifs. However, genes highly homologous to rcd1+ (encoding amino acids with >70% identity) are present at least in budding yeasts, plants, nematodes, and humans. Cells with rcd1+ deleted are sterile if sexual development is induced by nitrogen starvation but fertile if it is induced by glucose starvation. This results largely from a defect in nitrogen starvation-invoked induction of ste11+, a key transcriptional factor gene required for the onset of sexual development. The striking conservation of the gene throughout eukaryotes may suggest the presence of an evolutionarily conserved differentiation controlling system.
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Okazaki, N; Okazaki, K; Watanabe, Y; Kato-Hayashi, M; Yamamoto, M; Okayama, H. 1998. Novel factor highly conserved among eukaryotes controls sexual development in fission yeast. Mol. Cell. Biol. 18(2):887-95
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TR
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Rel
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<a target="_blank" class="awithout" href="http://pfam.xfam.org/family/PF00554">PFAM</a> (0): The Rel homology domain (RHD) is a protein domain found in a family of eukaryotic transcription factors, which includes NF-κB, NFAT, among others. The RHD is composed of two immunoglobulin-like beta barrel subdomains that grip the DNA in the major groove. The N-terminal specificity domain resembles the core domain of the p53 transcription factor, and contains a recognition loop that interacts with DNA bases. The C-terminal dimerization domain contains the site for interaction with I-kappaB.
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Müller, CW; Rey, FA; Sodeoka, M; Verdine, GL; Harrison, SC. 1995. Structure of the NF-kappa B p50 homodimer bound to DNA. Nature. 373(6512):311-7,"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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RF-X
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Reith et al (1990): RFX is a regulatory factor which binds to the X box of MHC class II genes and is essential for their expression. The DNA-binding domain of RFX is the central domain of the protein and binds ssDNA as either a monomer or homodimer.
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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,"Reith, W; Herrero-Sanchez, C; Kobr, M; Silacci, P; Berte, C; Barras, E; Fey, S; Mach, B. 1990. MHC class II regulatory factor RFX has a novel DNA-binding domain and a functionally independent dimerization domain. Genes Dev. 4(9):1528-40"
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TF
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RKD
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According to (Chardin et al., 2014), the plant specific RWP-RK TF Family can be divided into the two subfamilies NLP (NIN-like proteins) and RKD (RWP-RK domain proteins). Proteins belonging to the subfamily NLP provide an additional PB1 (Phox and Bem 1) domain at their C-terminus (Chardin et al., 2014; Wu et al., 2020). RWP-RK proteins are involved in response to nitrate availability and in nodule interception (Wu et al., 2020).
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Chardin, C., Girin, T., Roudier, F., Meyer, C., & Krapp, A. (2014). The plant RWP-RK transcription factors: key regulators of nitrogen responses and of gametophyte development. Journal of Experimental Botany, 65(19), 5577–5587. https://doi.org/10.1093/jxb/eru261,"Wu, Z., Liu, H., Huang, W., Yi, L., Qin, E., Yang, T., Wang, J., & Qin, R. (2020). Genome-Wide Identification, Characterization, and Regulation of RWP-RK Gene Family in the Nitrogen-Fixing Clade. Plants, 9(9), 1178. https://doi.org/10.3390/plants9091178"
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TF
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RRN3
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Yamamoto et al (1996): RRN3 is one of the RRN genes specifically required for the transcription of rDNA by RNA polymerase I (Pol I) in Saccharomyces cerevisiae.
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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,"Yamamoto, RT; Nogi, Y; Dodd, JA; Nomura M. 1996. RRN3 gene of Saccharomyces cerevisiae encodes an essential RNA polymerase I transcription factor which interacts with the polymerase independently of DNA template. EMBO J. 15(15):3964-73"
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TR
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Runt
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<a target="_blank" class="awithout" href="http://pfam.xfam.org/family/PF00853">PFAM</a> (0): The Runt domain is responsible for DNA-binding and protein-protein interaction.
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Kagoshima, H; Shigesada, K; Satake, M; Ito, Y; Miyoshi, H; Ohki, M; Pepling, M; Gergen, P. 1993. The Runt domain identifies a new family of heteromeric transcriptional regulators. Trends Genet. 9(10):338-41,"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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RWP-RK
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Schauser et al (2005): Genetic studies in Lotus japonicus and pea have identified Nin as a core symbiotic gene required for establishing symbiosis between legumes and nitrogen fixing bacteria collectively called Rhizobium. Sequencing of additional Lotus cDNAs combined with analysis of genome sequences from Arabidopsis and rice reveals that Nin homologues in all three species constitute small gene families. In total, the Arabidopsis and rice genomes encode nine and three NIN-like proteins (NLPs), respectively. We present here a bioinformatics analysis and prediction of NLP evolution. On a genome scale we show that in Arabidopsis, this family has evolved through segmental duplication rather than through tandem amplification. Alignment of all predicted NLP protein sequences shows a composition with six conserved modules. In addition, Lotus and pea NLPs contain segments that might characterize NIN proteins of legumes and be of importance for their function in symbiosis. The most conserved region in NLPs, the RWP-RK domain, has secondary structure predictions consistent with DNA binding properties. This motif is shared by several other small proteins in both Arabidopsis and rice. In rice, the RWP-RK domain sequences have diversified significantly more than in Arabidopsis. Database searches reveal that, apart from its presence in Arabidopsis and rice, the motif is also found in the algae Chlamydomonas and in the slime mold Dictyostelium discoideum. Thus, the origin of this putative DNA binding region seems to predate the fungus-plant divide.
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Schauser, L; Roussis, A; Stiller, J; Stougaard, J. 1999. A plant regulator controlling development of symbiotic root nodules. Nature 402(6758):191-5
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TF
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S1Fa-like
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Zhou et al (1995): A cDNA encoding a specific binding activity for the tissue-specific negative cis-element S1F binding site of spinach rps1 was isolated from a spinach cDNA expression library. This cDNA of 0.7 kb encodes an unusual small peptide of only 70 amino acids, with a basic domain which contains a nuclear localization signal and a putative DNA binding helix. This protein, named S1Fa, is highly conserved between dicotyledonous and monocotyledonous plants and may represent a novel class of DNA binding proteins. The corresponding mRNA is accumulated more in roots and in etiolated seedlings than in green leaves. This expression pattern is correlated with the tissue-specific function of the S1F binding site which represses the rps1 promoter preferentially in roots and in etiolated plants.
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Zhou, DX; Bisanz-Seyer, C; Mache, R. 1995. Molecular cloning of a small DNA binding protein with specificity for a tissue-specific negative element within the rps1 promoter. Nucleic Acids Res. 23(7):1165-9
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TF
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SAP
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Byzova et al (1999): A recessive mutation in the Arabidopsis STERILE APETALA (SAP) causes severe aberrations in inflorescence and flower and ovule development. In sap flowers, sepals are carpelloid, petals are short and narrow or absent, and anthers are degenerated. Megasporogenesis, the process of meiotic divisions preceding the female gametophyte formation, is arrested in sap ovules during or just after the first meiotic division. More severe aberrations were observed in double mutants between sap and mutant alleles of the floral homeotic gene APETALA2 (AP2) suggesting that both genes are involved in the initiation of female gametophyte development. Together with the organ identity gene AGAMOUS (AG) SAP is required for the maintenance of floral identity acting in a manner similar to APETALA1. In contrast to the outer two floral organs in sap mutant flowers, normal sepals and petals develop in ag/sap double mutants, indicating that SAP negatively regulates AG expression in the perianth whorls. This supposed cadastral function of SAP is supported by in situ hybridization experiments showing ectopic expression of AG in the sap mutant. We have cloned the SAP gene by transposon tagging and revealed that it encodes a novel protein with sequence motifs, that are also present in plant and animal transcription regulators. Consistent with the mutant phenotype, SAP is expressed in inflorescence and floral meristems, floral organ primordia, and ovules. Taken together, we propose that SAP belongs to a new class of transcription regulators essential for a number of processes in Arabidopsis flower development.
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Byzova, MV; Franken, J; Aarts, MG; de Almeida-Engler, J; Engler, G; Mariani, C; Van Lookeren Campagne, MM; Angenent, GC. 1999. Arabidopsis STERILE APETALA, a multifunctional gene regulating inflorescence, flower, and ovule development. Genes Dev. 13(8):1002-14
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TF
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SBP
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Cardon et al (1999): The Arabidopsis thaliana SPL gene family represents a group of structurally diverse genes encoding putative transcription factors found apparently only in plants. The distinguishing characteristic of the SPL gene family is the SBP-box encoding a conserved protein domain of 76 amino acids in length, the SBP-domain, which is responsible for the interaction with DNA. We present here characterisation of 12 members of the SPL gene family. These genes show highly diverse genomic organisations and are found scattered over the Arabidopsis genome. Some SPL genes are constitutively expressed, while transcriptional activity of others is under developmental control. Based on phylogenetic reconstruction, gene structure and expression patterns, they can be divided into subfamilies. In addition to the Arabidopsis SPL genes, we isolated and determined the sequences of three SBP-box genes from Antirrhinum majus and seven from Zea mays.
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Cardon, G; Höhmann, S; Klein, J; Nettesheim, K; Saedler, H; Huijser, P. 1999. Molecular characterisation of the Arabidopsis SBP-box genes. Gene. 237(1):91-104,"Guo, AY; Zhu, QH; Gu, X; Ge, S; Yang, J; Luo, J. 2008. Genome-wide identification and evolutionary analysis of the plant specific SBP-box transcription factor family. Gene 418(1-2):1-8","Klein, J; Saedler, H; Huijser, P. 1996. A new family of DNA binding proteins includes putative transcriptional regulators of the Antirrhinum majus floral meristem identity gene SQUAMOSA. Mol. Gen. Genet. 250(1):7-16"
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TF
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SET
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Marmorstein (2003): The methylation of lysine residues on histone tails is catalyzed by proteins containing a conserved SET domain. A recent flurry of structures of SET domain proteins has revealed a new protein fold and a scaffold for understanding catalysis and substrate binding by these enzymes. The prospect that histone methylation might form an epigenetic code and the implicated involvement of SET domain proteins in cancer assures that structure-function studies of these enzymes will continue until their detailed mechanism of action is determined.
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Marmorstein, R. 2003. Structure of SET domain proteins: a new twist on histone methylation. Trends Biochem. Sci. 28(2):59-62,"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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Sigma70-like
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Allison (2000): Expression of plastid genes is controlled at both transcriptional and post-transcriptional levels in response to developmental and environmental signals. In many cases this regulation is mediated by nuclear-encoded proteins acting in concert with the endogenous plastid gene expression machinery. Transcription in plastids is accomplished by two distinct RNA polymerase enzymes, one of which resembles eubacterial RNA polymerases in both subunit structure and promoter recognition properties. The holoenzyme contains a catalytic core composed of plastid-encoded subunits, assembled with a nuclear-encoded promoter-specificity factor, sigma. Based on examples of transcriptional regulation in bacteria, it is proposed that differential activation of sigma factors may provide the nucleus with a mechanism to control expression of groups of plastid genes. Hence, much effort has focused on identifying and characterizing sigma-like factors in plants. While fractionation studies had identified several candidate sigma factors in purified RNA polymerase preparations, it was only 4 years ago that the first sigma factor genes were cloned from two photosynthetic eukaryotes, both of which were red algae. More recently this achievement has extended to the identification of families of sigma-like factor genes from several species of vascular plants. Now, efforts in the field are directed at understanding the roles in plastid transcription of each member of the rapidly expanding plant sigma factor gene family. Recent results suggest that accumulation of individual sigma-like factors is controlled by light, by plastid type and/or by a particular stage of chloroplast development. These data mesh nicely with accumulating evidence that the core sigma-binding regions of plastid promoters mediate regulated transcription in response to light-regime and plastid type or developmental state. In this review I will outline progress made to date in identifying and characterizing the sigma-like factors of plants, and in dissecting their potential roles in chloroplast gene expression.
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Allison, LA. 2000. The role of sigma factors in plastid transcription. Biochimie 82(6-7):537-48,"Paget, MS; Helmann, JD. 2003. The sigma70 family of sigma factors. Genome Biol. 4(1):203","Sriraman, P; Silhavy, D; Maliga, P. 1998. Transcription from heterologous rRNA operon promoters in chloroplasts reveals requirement for specific activating factors. Plant Physiol. 117(4):1495-9"
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TR
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Sin3
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<a target="_blank" class="awithout" href="http://pfam.xfam.org/family/PF02671">PFAM</a> (0): This family contains the paired amphipathic helix repeat. The family contains the yeast SIN3 gene. This repeat may be distantly related to the helix-loop-helix motif, which mediates protein-protein interactions.
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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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Sir2
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<a target="_blank" class="awithout" href="http://pfam.xfam.org/family/PF02146">PFAM</a> (0): Sirtuins are a class of proteins that possess either mono-ADP-ribosyltransferase, or deacylase activity and have been implicated in a wide range of cellular processes, including transcription. The human Sirt7 is involved in rRNA transcription in the nucleolus.
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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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SOH1
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Fan et al (1996): The soh1, soh2 and soh4 mutants were isolated as suppressors of the temperature-dependent growth of the hyperrecombination mutant hpr1 of Saccharomyces cerevisiae. Cloning and sequence analysis of these suppressor genes has unexpectedly shown them to code for components of the RNA polymerase II transcription complex. SOH2 is identical to RPB2, which encodes the second largest subunit of RNA polymerase II, and SOH4 is the same as SUA7, encoding the yeast transcription initiation factor TFIIB. SOH1 encodes a novel 14-kD protein with limited sequence similarity to RNA polymerases. Interestingly, SOH1 not only interacts with factors involved in DNA repair, but transcription as well. Thus, the Soh1 protein may serve to couple these two processes. The Soh1 protein interacts with a DNA repair protein, Rad5p, in a two-hybrid system assay. Soh1p may functionally interact with components of the RNA polymerase II complex as suggested from the synthetic lethality observed in soh1 rpb delta 104, soh1 soh2-1 (rpb2), and soh1 soh4 (sua7) double mutants. Because mutations in SOH1, RPB2 and SUA7 suppress the hyperrecombination phenotype of hpr1 mutants, this suggests a link between recombination in direct repeats and transcription.
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Fan, HY; Cheng, KK; Klein, HL. 1996. Mutations in the RNA polymerase II transcription machinery suppress the hyperrecombination mutant hpr1 delta of Saccharomyces cerevisiae. Genetics 142(3):749-59
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TR
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SRS
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Fridborg et al (2001): The current model of gibberellin (GA) signal transduction is based on a derepressible system and a number of candidate negative regulators have been identified in Arabidopsis. We previously have reported the identification of the Arabidopsis gene SHORT INTERNODES (SHI) that causes suppression of GA responses when constitutively activated. In this paper, we show by using reporter gene analysis that the SHI gene is expressed in young organs, e.g. shoot apices and root tips. The model predicts a suppressor of GA responses to be active in these tissues to prevent premature growth or development. To study the effect of SHI on GA signaling, we used a functional assay that measures effects of signaling components on a well-defined GA response; the up-regulation of alpha-amylase in barley (Hordeum vulgare) aleurones in response to GA treatment. We found that SHI was able to specifically block the activity of a high-isoelectric point alpha-amylase promoter following GA(3) treatment, which further supports that SHI is a suppressor of GA responses. We have identified two putative loss-of-function insertion alleles of SHI and lines homozygous for either of the new alleles show no phenotypic deviations from wild type. Because SHI belongs to a gene family consisting of nine members, we suggest that SHI and the SHI-related genes are functionally redundant. We also show that a functional ERECTA allele is able to partly suppress the dwarfing effect of the shi gain-of-function mutation, suggesting that the erecta mutation harbored by the Landsberg erecta ecotype is an enhancer of the shi dwarf phenotype.
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Fridborg, I; Kuusk, S; Robertson, M; Sundberg, E. 2001. The Arabidopsis protein SHI represses gibberellin responses in Arabidopsis and barley. Plant Physiol. 127(3):937-48
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TF
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SWI/SNF_BAF60b
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Kussie et al (1996): The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.
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Bennett-Lovsey, R; Hart, SE; Shirai, H; Mizuguchi, K. 2002. The SWIB and the MDM2 domains are homologous and share a common fold. Bioinformatics 18(4):626-30,"Kussie, PH; Gorina, S; Marechal, V; Elenbaas, B; Moreau, J; Levine, AJ; Pavletich, NP. 1996. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274(5289):948-53"
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TR
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SWI/SNF_SNF2
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Eisen et al (1995): The SNF2 family of proteins includes representatives from a variety of species with roles in cellular processes such as transcriptional regulation (e.g. MOT1, SNF2 and BRM), maintenance of chromosome stability during mitosis (e.g. lodestar) and various aspects of processing of DNA damage, including nucleotide excision repair (e.g. RAD16 and ERCC6), recombinational pathways (e.g. RAD54) and post-replication daughter strand gap repair (e.g. RAD5). This family also includes many proteins with no known function. To better characterize this family of proteins we have used molecular phylogenetic techniques to infer evolutionary relationships among the family members. We have divided the SNF2 family into multiple subfamilies, each of which represents what we propose to be a functionally and evolutionarily distinct group. We have then used the subfamily structure to predict the functions of some of the uncharacterized proteins in the SNF2 family. We discuss possible implications of this evolutionary analysis on the general properties and evolution of the SNF2 family.
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Bork, P; Koonin, EV. 1993. An expanding family of helicases within the 'DEAD/H' superfamily. Nucleic Acids Res. 21(3):751-2,"Eisen, JA; Sweder, KS; Hanawalt, PC. 1995. Evolution of the SNF2 family of proteins: subfamilies with distinct sequences and functions. Nucleic Acids Res. 23(14):2715-23","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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SWI/SNF_SWI3
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Da et al (2006): The SWIRM domain is a module found in the Swi3 and Rsc8 subunits of SWI/SNF-family chromatin remodeling complexes, and the Ada2 and BHC110/LSD1 subunits of chromatin modification complexes. Here we report the high-resolution crystal structure of the SWIRM domain from Swi3 and characterize the in vitro and in vivo function of the SWIRM domains from Saccharomyces cerevisiae Swi3 and Rsc8. The Swi3 SWIRM forms a four-helix bundle containing a pseudo 2-fold axis and a helix-turn-helix motif commonly found in DNA-binding proteins. We show that the Swi3 SWIRM binds free DNA and mononucleosomes with high and comparable affinity and that a subset of Swi3 substitution mutants that display growth defects in vivo also show impaired DNA-binding activity in vitro, consistent with a nucleosome targeting function of this domain. Genetic and biochemical studies also reveal that the Rsc8 and Swi3 SWIRM domains are essential for the proper assembly and in vivo functions of their respective complexes. Together, these studies identify the SWIRM domain as an essential multifunctional module for the regulation of gene expression.
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Da, G; Lenkart, J; Zhao, K; Shiekhattar, R; Cairns, BR; Marmorstein, R. 2006. Structure and function of the SWIRM domain, a conserved protein module found in chromatin regulatory complexes. Proc. Natl. Acad. Sci. U.S.A. 103(7):2057-62
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TR
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TAFII250
|
Lysine acetyltransferases or histone acetyltransferases (HATs) together with histone deacetylases (HDACs), are responsible for reversible acetylation of histones and are found in eukaryotes in at least four TR families, namely MYST (MOZ, Ybf2/Sas3, Sas2 and TIP60), CBP (p300/CREB-binding protein), TAFII250 (TATA-binding protein associated factor) and GNAT (GCN5-related N-terminal acetyltransferase) (Boycheva et al., 2014; Pandey, 2002; Uhrig et al., 2017). HATs function as transcriptional regulators by having different regulatory effects on gene expression in plants, animals and fungi, indicating a high conservation of these proteins and their functions (Pandey, 2002). Especially in land plants, due to their sessile lifestyle, chromatin modifications provide an important mechanism in adapting to environmental stresses (Boycheva et al., 2014). In non-photosynthetic eukaryotes, monocots, and dicots an average of one to two members of the HAT subfamily TAFII250 can be found (Uhrig et al., 2017). Furthermore, they are also present in early photosynthetic eukaryotes as red algae (Uhrig et al., 2017). Functions such as participation in light response and the phytochrome pathway could be observed (Boycheva et al., 2014).
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Boycheva, I., Vassileva, V., & Iantcheva, A. (2014). Histone Acetyltransferases in Plant Development and Plasticity. Current Genomics, 15(1), 28–37. https://doi.org/10.2174/138920291501140306112742,"Pandey, R. (2002). Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes. Nucleic Acids Research, 30(23), 5036–5055. https://doi.org/10.1093/nar/gkf660","Uhrig, R. G., Schläpfer, P., Mehta, D., Hirsch-Hoffmann, M., & Gruissem, W. (2017). Genome-scale analysis of regulatory protein acetylation enzymes from photosynthetic eukaryotes. BMC Genomics, 18(1), 514. https://doi.org/10.1186/s12864-017-3894-0"
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TR
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