A new family of plant transcription factors displays a novel ssDNA-binding surface

Desveaux, Darrell; Allard, Julie; Brisson, Normand; Sygusch, J.

doi:10.1038/nsb814

Cited by 94 publications

(119 citation statements)

References 36 publications

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“…The data were processed, indexed and scaled using either HKL-2000 (Otwinowski & Minor, 1997) or XDS (Kabsch, 2010) and SCALA (Evans, 1993). The structures of WHY1 and WHY2 were solved by molecular replacement using PHENIX (Adams et al, 2010) with the crystal structures of the potato WHY1 (PDB entry 1l3a; Desveaux et al, 2002) and WHY2 (PDB entry 3n1h; Cappadocia et al, 2010) as search models, respectively. The structure of WHY3 was also solved by molecular replacement using the refined structure of WHY1 as a search model.…”

Section: X-ray Data Collection Structure Determination and Refinementmentioning

confidence: 99%

“…The crystal structures of the Solanum tuberosum (potato) WHY1 and WHY2 proteins were solved in the free form (Desveaux et al, 2002;Cappadocia et al, 2008Cappadocia et al, , 2010. These structures revealed that both chloroplast-directed and mitochondria-directed Whirly proteins assemble into tetramers with C4 symmetry.…”

Section: Introductionmentioning

confidence: 99%

“…Whirly proteins are mainly found in the plant kingdom, where they localize to either chloroplasts (specialized mature plastids responsible for photosynthesis) or mitochondria (reviewed in Desveaux et al, 2005). In solution, the recombinant proteins form tetramers (Desveaux et al, 2002;Cappadocia et al, 2010) that bind single-stranded DNA with low sequence specificity (Cappadocia et al, 2010). In the absence of the chloroplast-directed Whirly proteins, the plastid genome of both Arabidopsis thaliana and Zea mays (maize) becomes unstable and accumulates DNA rearrangements that contain microhomologies at their endpoint junction (Maré chal et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

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A family portrait: structural comparison of the Whirly proteins fromArabidopsis thalianaandSolanum tuberosum

Cappadocia

Parent

Sygusch

et al. 2013

Acta Crystallogr F Struct Biol Cryst Commun

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PDB references: WHY1, 4koo; WHY2, 4kop; WHY3, 4koq DNA double-strand breaks are highly detrimental genomic lesions that routinely arise in genomes. To protect the integrity of their genetic information, all organisms have evolved specialized DNA-repair mechanisms. Whirly proteins modulate DNA repair in plant chloroplasts and mitochondria by binding single-stranded DNA in a non-sequence-specific manner. Although most of the results showing the involvement of the Whirly proteins in DNA repair have been obtained in Arabidopsis thaliana, only the crystal structures of the potato Whirly proteins WHY1 and WHY2 have been reported to date. The present report of the crystal structures of the three Whirly proteins from A. thaliana (WHY1, WHY2 and WHY3) reveals that these structurally similar proteins assemble into tetramers. Furthermore, structural alignment with a potato WHY2-DNA complex reveals that the residues in these proteins are properly oriented to bind single-stranded DNA in a non-sequence-specific manner.

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Section: X-ray Data Collection Structure Determination and Refinementmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A family portrait: structural comparison of the Whirly proteins fromArabidopsis thalianaandSolanum tuberosum

Cappadocia

Parent

Sygusch

et al. 2013

Acta Crystallogr F Struct Biol Cryst Commun

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“…It has been proposed that this protein might bind to melted promoter regions to modulate transcriptional activities. The interaction of StWHY1 with the PR-10a promoter was mapped to a region termed the elicitor response element (ERE) for elicitor-induced gene expression (Després et al, 1995;Desveaux et al, 2000Desveaux et al, , 2002. The Arabidopsis genome encodes three WHY proteins: AtWHY1 and AtWHY3 contain plastid-targeting signal, whereas AtWHY2 localizes to mitochondria (Krause et al, 2005).…”

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confidence: 99%

The Single-Stranded DNA-Binding Protein WHIRLY1 Represses WRKY53 Expression and Delays Leaf Senescence in a Developmental Stage-Dependent Manner in Arabidopsis

et al. 2013

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Leaf senescence in plants involves both positive and negative transcriptional regulation. In this work, we show evidence for the single-stranded DNA-binding protein WHIRLY1 (WHY1) that functions as an upstream suppressor of WRKY53 in a developmental stage-dependent manner during leaf senescence in Arabidopsis (Arabidopsis thaliana). The why1 mutant displayed an early-senescence phenotype. In this background, the expression levels of both WRKY53 and the senescenceassociated protease gene SAG12 increased. WHY1 bound to the sequence region that contains an elicitor response element motif-like sequence, GNNNAAATT, plus an AT-rich telomeric repeat-like sequence in the WRKY53 promoter in in vivo and in vitro mutagenesis assays as well as in a chromatin immunoprecipitation assay. This binding to the promoter of WRKY53 was regulated in a developmental stage-dependent manner, as verified by chromatin immunoprecipitation-polymerase chain reaction assay. This direct interaction was further determined by a transient expression assay in which WHY1 repressed b-GLUCURONIDASE gene expression driven by the WRKY53 promoter. Genetic analysis of double mutant transgenic plants revealed that WHY1 overexpression in the wrky53 mutant (oeWHY1wrky53) had no effect on the stay-green phenotype of the wrky53 mutant, while a WHY1 knockout mutant in the wrky53 mutant background (why1wrky53) generated subtle change in the leaf yellow/green phenotype. These results suggest that WHY1 was an upstream regulator of WRKY53 during leaf senescence.

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“…Analyses of the crystal structure of WHIRLY proteins revealed that they form tetramers [68] and that these tetramers can also assemble into 24-mers [69,70]. The 24-oligomers of WHIRLY1 have been isolated from chloroplasts [70] and they are likely to be the structures that bind to the thylakoids.…”

Section: The Whirly Family Of Proteinsmentioning

confidence: 99%

The functions of WHIRLY1 and REDOX-RESPONSIVE TRANSCRIPTION FACTOR 1 in cross tolerance responses in plants: a hypothesis

Foyer

Karpińska

Krupinska

2014

Phil. Trans. R. Soc. B

119

112

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Chloroplasts are important sensors of environment change, fulfilling key roles in the regulation of plant growth and development in relation to environmental cues. Photosynthesis produces a repertoire of reductive and oxidative (redox) signals that provide information to the nucleus facilitating appropriate acclimation to a changing light environment. Redox signals are also recognized by the cellular innate immune system allowing activation of non-specific, stress-responsive pathways that underpin cross tolerance to biotic–abiotic stresses. While these pathways have been intensively studied in recent years, little is known about the different components that mediate chloroplast-to-nucleus signalling and facilitate cross tolerance phenomena. Here, we consider the properties of the WHIRLY family of proteins and the REDOX-RESPONSIVE TRANSCRIPTION FACTOR 1 (RRTF1) in relation to chloroplast redox signals that facilitate the synergistic co-activation of gene expression pathways and confer cross tolerance to abiotic and biotic stresses. We propose a new hypothesis for the role of WHIRLY1 as a redox sensor in chloroplast-to-nucleus retrograde signalling leading to cross tolerance, including acclimation and immunity responses. By virtue of its association with chloroplast nucleoids and with nuclear DNA, WHIRLY1 is an attractive candidate coordinator of the expression of photosynthetic genes in the nucleus and chloroplasts. We propose that the redox state of the photosynthetic electron transport chain triggers the movement of WHIRLY1 from the chloroplasts to the nucleus, and draw parallels with the regulation of NONEXPRESSOR OF PATHOGENESIS-RELATED GENES 1 (NPR1).

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A new family of plant transcription factors displays a novel ssDNA-binding surface

Cited by 94 publications

References 36 publications

A family portrait: structural comparison of the Whirly proteins fromArabidopsis thalianaandSolanum tuberosum

A family portrait: structural comparison of the Whirly proteins fromArabidopsis thalianaandSolanum tuberosum

The Single-Stranded DNA-Binding Protein WHIRLY1 Represses WRKY53 Expression and Delays Leaf Senescence in a Developmental Stage-Dependent Manner in Arabidopsis

The functions of WHIRLY1 and REDOX-RESPONSIVE TRANSCRIPTION FACTOR 1 in cross tolerance responses in plants: a hypothesis

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