Recombinant Whirly1 translocates from transplastomic chloroplasts to the nucleus

Isemer, Rena; Mulisch, Maria; Schäfer, Anke; Kirchner, Stefan; Koop, Hans‐Ulrich; Krupinska, Karin

doi:10.1016/j.febslet.2011.11.029

Cited by 112 publications

(117 citation statements)

References 20 publications

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“…PTM, a membrane-bound transcription factor that localizes to the chloroplast outer envelope by four transmembrane domains at its C terminus, has been found to be activated by proteolytic cleavage of the transmembrane domains and to transmit multiple retrograde chloroplast signals to the nucleus . In addition, Whirly1 was shown to be dually located in both the chloroplasts and nucleus of the same cell with the same molecular size and to affect the expression of target genes such as PR1 in the nucleus (Isemer et al, 2012). Similarly, it was reported that GFP fusion proteins could be transported from chloroplasts to the cytoplasm upon biotic and abiotic stresses (Kwon et al, 2013).…”

Section: Discussionmentioning

confidence: 96%

“…1D) exists in the cytoplasm, it is likely that the chloroplast-localized ZmVDEm could be transported back into the cytoplasm. Interestingly, several chloroplast proteins involved in cytoplasm and/or nuclear localization have been reported as retrograde signals to modulate nuclear gene expression (Chen et al, 2010;Sun et al, 2011;Isemer et al, 2012). PTM, a membrane-bound transcription factor that localizes to the chloroplast outer envelope by four transmembrane domains at its C terminus, has been found to be activated by proteolytic cleavage of the transmembrane domains and to transmit multiple retrograde chloroplast signals to the nucleus .…”

Section: Discussionmentioning

confidence: 99%

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A Violaxanthin Deepoxidase Interacts with a Viral Suppressor of RNA Silencing to Inhibit Virus Amplification

et al. 2017

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RNA silencing plays a critical role against viral infection. To counteract this antiviral silencing, viruses have evolved various RNA silencing suppressors. Meanwhile, plants have evolved counter-counter defense strategies against RNA silencing suppression (RSS). In this study, the violaxanthin deepoxidase protein of maize (Zea mays), ZmVDE, was shown to interact specifically with the helper component-proteinase (HC-Pro; a viral RNA silencing suppressor) of Sugarcane mosaic virus (SCMV) via its mature protein region by yeast two-hybrid assay, which was confirmed by coimmunoprecipitation in Nicotiana benthamiana cells. It was demonstrated that amino acids 101 to 460 in HC-Pro and the amino acid glutamine-292 in ZmVDE mature protein were essential for this interaction. The mRNA levels of ZmVDE were down-regulated 75% to 65% at an early stage of SCMV infection. Interestingly, ZmVDE, which normally localized in the chloroplasts and cytoplasm, could relocalize to HC-Pro-containing aggregate bodies in the presence of HC-Pro alone or SCMV infection. In addition, ZmVDE could attenuate the RSS activity of HC-Pro in a specific protein interaction-dependent manner. Subsequently, transient silencing of the ZmVDE gene facilitated SCMV RNA and coat protein accumulation. Taken together, our results suggest that ZmVDE interacts with SCMV HC-Pro and attenuates its RSS activity, contributing to decreased SCMV accumulation. This study demonstrates that a host factor can be involved in secondary defense responses against viral infection in monocot plants.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

A Violaxanthin Deepoxidase Interacts with a Viral Suppressor of RNA Silencing to Inhibit Virus Amplification

et al. 2017

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“…3C) suggested that this nuclear WHY1 resembled the cleaved plastid WHY1 protein (Grabowski et al, 2008;Isemer et al, 2012). Furthermore, WHY1 formed a complex only with the sense DNA strand but not with the antisense DNA strand (Fig.…”

Section: The Why1 Protein Binds To the Promoter Of Wrky53mentioning

confidence: 88%

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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“…The dual location in plastids and the nucleus of the same cell makes WHIRLY1 an ideal candidate for information trafficking from plastids to the nucleus. The translocation of WHIRLY1 from chloroplasts to the nucleus has been demonstrated recently in studies using transplastomic tobacco plants synthesizing an HA-tagged version of WHIRLY1 at the 70S ribosomes of the organelles [57]. The tagged WHIRLY1 was detected in the nucleus, where it stimulated expression of PR genes [57].…”

Section: The Whirly Family Of Proteinsmentioning

confidence: 86%

“…Plants have a small family of single-stranded DNA binding proteins called WHIRLY that are also involved in the control of defence gene expression [56,57]. Although most plant species have two members, some species including Arabidopsis thaliana have three WHIRLY proteins.…”

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

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121

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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Recombinant Whirly1 translocates from transplastomic chloroplasts to the nucleus

Cited by 112 publications

References 20 publications

A Violaxanthin Deepoxidase Interacts with a Viral Suppressor of RNA Silencing to Inhibit Virus Amplification

A Violaxanthin Deepoxidase Interacts with a Viral Suppressor of RNA Silencing to Inhibit Virus Amplification

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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