A SAM oligomerization domain shapes the genomic binding landscape of the LEAFY transcription factor

Sayou, Camille; Nanao, Max H.; Jamin, Marc; Posé, David; Thévenon, Emmanuel; Grégoire, Laura; Tichtinsky, Gabrielle; Denay, Grégoire; Ott, Felix; Peirats‐Llobet, Marta; Schmid, Markus; Dumas, Renaud; Parcy, François

doi:10.1038/ncomms11222

Cited by 89 publications

(156 citation statements)

References 66 publications

(108 reference statements)

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“…The resulting model shows a head‐to‐tail helical oligomer [Fig. (B)], similar to the oligomeric structures of several other SAM domains in which oligomers of SAM domains form a right‐handed helix that contains ∼6 protomers per turn. While these structures differ in their helical pitch (primarily determined by the angle between promoters), this helical form is likely adopted by many SAM oligomers .…”

Section: Resultsmentioning

confidence: 61%

“…SAM domains have been shown to mediate protein–protein, protein–RNA, and protein–lipid interactions . Furthermore, SAM domains can bind themselves symmetrically, as in the example of Eph4A which forms a homodimer, can bind other SAM domains (e.g., odin binding to EphA2, and Ste11 binding to Ste50), and can form long‐range homo‐oligomeric/polymeric structures . While it is generally accepted that the SAM domain is largely responsible for the oligomerization of TNKS1/2, the domain has not yet been structurally or biochemically characterized.…”

Section: Introductionmentioning

confidence: 99%

“…25 Furthermore, SAM domains can bind themselves symmetrically, as in the example of Eph4A which forms a homodimer, 26 can bind other SAM domains (e.g., odin binding to EphA2, and Ste11 binding to Ste50), [27][28][29] and can form long-range homo-oligomeric/polymeric structures. [30][31][32][33][34][35][36][37] While it is generally accepted that the SAM domain is largely responsible for the oligomerization of TNKS1/2, 38,39 the domain has not yet been structurally or biochemically characterized. It is still unknown whether the domain forms oligomers using multiple interfaces as observed for the SAM domain structure of EphB2 receptor, 40 homotypic oligomers with a single, distinct head-to-tail interface observed for other SAM polymers, 41 or utilizes some heretofore unobserved oligomeric topology.…”

Section: Introductionmentioning

confidence: 99%

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Structural insights into SAM domain‐mediated tankyrase oligomerization

DaRosa

Овчинников

et al. 2016

Protein Science

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Tankyrase 1 (TNKS1; a.k.a. ARTD5) and tankyrase 2 (TNKS2; a.k.a ARTD6) are highly homologous poly(ADP-ribose) polymerases (PARPs) that function in a wide variety of cellular processes including Wnt signaling, Src signaling, Akt signaling, Glut4 vesicle translocation, telomere length regulation, and centriole and spindle pole maturation. Tankyrase proteins include a sterile alpha motif (SAM) domain that undergoes oligomerization in vitro and in vivo. However, the SAM domains of TNKS1 and TNKS2 have not been structurally characterized and the mode of oligomerization is not yet defined. Here we model the SAM domain-mediated oligomerization of tankyrase. The structural model, supported by mutagenesis and NMR analysis, demonstrates a helical, homotypic head-to-tail polymer that facilitates TNKS self-association. Furthermore, we show that TNKS1 and TNKS2 can form (TNKS1 SAM-TNKS2 SAM) hetero-oligomeric structures mediated by their SAM domains. Though wild-type tankyrase proteins have very low solubility, model-based mutations of the SAM oligomerization interface residues allowed us to obtain soluble TNKS proteins. These structural insights will be invaluable for the functional and biophysical characterization of TNKS1/2, including the role of TNKS oligomerization in protein poly(ADP-ribosyl)ation (PARylation) and PARylation-dependent ubiquitylation.

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Section: Resultsmentioning

confidence: 61%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Structural insights into SAM domain‐mediated tankyrase oligomerization

DaRosa

Овчинников

et al. 2016

Protein Science

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“…One possible reason is that LFY and its homologs are highly evolutionally conserved throughout the plant kingdom and show no apparent similarity to other proteins (Maizel et al, 2005). Two conserved domains of LFY protein were distinguished and, respectively, named as the DBD domain (DNA Binding Domain), which located in the N-terminal and leads it bind to the semi-palindromic 19-bp DNA cis -elements of the genes regulated by itself (Sayou et al, 2014), and the SAM domain (Sterile Alpha Motif), which located in the C-terminal and determines the genomic binding landscape (Sayou et al, 2016). Such characteristic motifs were also found in EjLFY-1 ( Figure 3 ), suggesting its possible flowering regulator role in the flowering process of loquat.…”

Section: Discussionmentioning

confidence: 99%

Over-expression of EjLFY-1 Leads to an Early Flowering Habit in Strawberry (Fragaria × ananassa) and Its Asexual Progeny

et al. 2017

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As a master regulator involved in flower development, LEAFY-like gene has been demonstrated to play a key role in the flowering process regulation of angiosperms. Expression analysis of EjLFY-1, a LEAFY (LFY) homolog of loquat (Eriobotrya japonica Lindl.), indicated its participation in the regulation of flowering in loquat. To verify its function and potential value in the genetic engineering to shorten the juvenile phase, ectopic expression of EjLFY-1 in strawberry (Fragaria × ananassa) was achieved using Agrobacterium-mediated gene transfer of a plant expression vector with the loquat EjLFY-1 gene driven by the CaMV 35S promoter. Totally 59 plantlets were verified to be the transformants. The presence, expression and integration of EjLFY-1 in the transformants were assessed by PCR, quantitative real-time PCR and Southern blot, respectively. Constitutive expression of EjLFY-1 in strawberry accelerated the flowering process in strawberry with the shorten necessary period for flowering induction, development of flower and fruit set. While vegetative growth habits of the transformants in the first cropping season were consistent with the WT ones. Meanwhile, both the flowers and fruits of the transformants were also as same as those of the WT ones. Furthermore, the early-flowering habit was maintained in their asexual progeny, the runner plants. While with continuous asexual propagation, the clones showed a more strengthen early-flowering phenotype, such as the reduced vegetative growth and the abnormal floral organs in individual plantlets. These results demonstrated the function of this gene and at the same time provided us new insights into the utilization potential of such genes in the genetic engineering of perennial fruits.

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“…This suggests that, of the two Welwitschia LFY-like genes, WelLFY DBD has the closest DNA preferences to Arabidopsis LFY. We then used a SELEXseq approach (Zhao et al, 2009;Moyroud et al, 2011;Chahtane et al, 2013) to characterize the DNA-binding specificity of nearfull-length proteins (WelLFYD and WelNDLYD) that included their conserved N-terminal oligomerization domain (Sayou et al, 2016). Comparison of the logo of WelLFYD with that of AtLFYD (Chahtane et al, 2013) shows that the DNA-binding preferences of these two factors are very similar ( Fig.…”

Section: New Phytologistmentioning

confidence: 99%

A link between LEAFY and B‐gene homologues in Welwitschia mirabilis sheds light on ancestral mechanisms prefiguring floral development

et al. 2017

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Flowering plants evolved from an unidentified gymnosperm ancestor. Comparison of the mechanisms controlling development in angiosperm flowers and gymnosperm cones may help to elucidate the mysterious origin of the flower. We combined gene expression studies with protein behaviour characterization in Welwitschia mirabilis to test whether the known regulatory links between LEAFY and its MADS-box gene targets, central to flower development, might also contribute to gymnosperm reproductive development. We found that WelLFY, one of two LEAFY-like genes in Welwitschia, could be an upstream regulator of the MADS-box genes APETALA3/PISTILLATA-like (B-genes). We demonstrated that, even though their DNA-binding domains are extremely similar, WelLFY and its paralogue WelNDLY exhibit distinct DNA-binding specificities, and that, unlike WelNDLY, WelLFY shares with its angiosperm orthologue the capacity to bind promoters of Welwitschia B-genes. Finally, we identified several cis-elements mediating these interactions in Welwitschia and obtained evidence that the link between LFY homologues and B-genes is also conserved in two other gymnosperms, Pinus and Picea. Although functional approaches to investigate cone development in gymnosperms are limited, our state-of-the-art biophysical techniques, coupled with expression studies, provide evidence that crucial links, central to the control of floral development, may already have existed before the appearance of flowers.

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A SAM oligomerization domain shapes the genomic binding landscape of the LEAFY transcription factor

Cited by 89 publications

References 66 publications

Structural insights into SAM domain‐mediated tankyrase oligomerization

Structural insights into SAM domain‐mediated tankyrase oligomerization

Over-expression of EjLFY-1 Leads to an Early Flowering Habit in Strawberry (Fragaria × ananassa) and Its Asexual Progeny

A link between LEAFY and B‐gene homologues in Welwitschia mirabilis sheds light on ancestral mechanisms prefiguring floral development

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