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Redox regulation of PEP activity during seedling establishment in Arabidopsis thaliana

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Redox regulation of PEP activity during seedling establishment in Arabidopsis thaliana. / Diaz, Manuel ; Hernandez-Verdeja, Tamara; Kremnev, Dmitry et al.
In: Nature Communications, Vol. 9, 50, 03.01.2018.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Diaz, M, Hernandez-Verdeja, T, Kremnev, D, Crawford, T, Dubreuil, C & Strand, A 2018, 'Redox regulation of PEP activity during seedling establishment in Arabidopsis thaliana', Nature Communications, vol. 9, 50. https://doi.org/10.1038/s41467-017-02468-2

APA

Diaz, M., Hernandez-Verdeja, T., Kremnev, D., Crawford, T., Dubreuil, C., & Strand, A. (2018). Redox regulation of PEP activity during seedling establishment in Arabidopsis thaliana. Nature Communications, 9, Article 50. https://doi.org/10.1038/s41467-017-02468-2

Vancouver

Diaz M, Hernandez-Verdeja T, Kremnev D, Crawford T, Dubreuil C, Strand A. Redox regulation of PEP activity during seedling establishment in Arabidopsis thaliana. Nature Communications. 2018 Jan 3;9:50. doi: 10.1038/s41467-017-02468-2

Author

Diaz, Manuel ; Hernandez-Verdeja, Tamara ; Kremnev, Dmitry et al. / Redox regulation of PEP activity during seedling establishment in Arabidopsis thaliana. In: Nature Communications. 2018 ; Vol. 9.

Bibtex

@article{eaa0d47220e845efaff7b0468c3e57c0,
title = "Redox regulation of PEP activity during seedling establishment in Arabidopsis thaliana",
abstract = "Activation of the plastid-encoded RNA polymerase is tightly controlled and involves a network of phosphorylation and, as yet unidentified, thiol-mediated events. Here, we characterize PLASTID REDOX INSENSITIVE2, a redox-regulated protein required for full PEP-driven transcription. PRIN2 dimers can be reduced into the active monomeric form by thioredoxins through reduction of a disulfide bond. Exposure to light increases the ratio between the monomeric and dimeric forms of PRIN2. Complementation of prin2-2 with different PRIN2 protein variants demonstrates that the monomer is required for light-activated PEP-dependent transcription and that expression of the nuclear-encoded photosynthesis genes is linked to the activity of PEP. Activation of PEP during chloroplast development likely is the source of a retrograde signal that promotes nuclear LHCB expression. Thus, regulation of PRIN2 is the thiol-mediated mechanism required for full PEP activity, with PRIN2 monomerization via reduction by TRXs providing a mechanistic link between photosynthetic electron transport and activation of photosynthetic gene expression.",
author = "Manuel Diaz and Tamara Hernandez-Verdeja and Dmitry Kremnev and Tim Crawford and Carole Dubreuil and Asa Strand",
year = "2018",
month = jan,
day = "3",
doi = "10.1038/s41467-017-02468-2",
language = "English",
volume = "9",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Redox regulation of PEP activity during seedling establishment in Arabidopsis thaliana

AU - Diaz, Manuel

AU - Hernandez-Verdeja, Tamara

AU - Kremnev, Dmitry

AU - Crawford, Tim

AU - Dubreuil, Carole

AU - Strand, Asa

PY - 2018/1/3

Y1 - 2018/1/3

N2 - Activation of the plastid-encoded RNA polymerase is tightly controlled and involves a network of phosphorylation and, as yet unidentified, thiol-mediated events. Here, we characterize PLASTID REDOX INSENSITIVE2, a redox-regulated protein required for full PEP-driven transcription. PRIN2 dimers can be reduced into the active monomeric form by thioredoxins through reduction of a disulfide bond. Exposure to light increases the ratio between the monomeric and dimeric forms of PRIN2. Complementation of prin2-2 with different PRIN2 protein variants demonstrates that the monomer is required for light-activated PEP-dependent transcription and that expression of the nuclear-encoded photosynthesis genes is linked to the activity of PEP. Activation of PEP during chloroplast development likely is the source of a retrograde signal that promotes nuclear LHCB expression. Thus, regulation of PRIN2 is the thiol-mediated mechanism required for full PEP activity, with PRIN2 monomerization via reduction by TRXs providing a mechanistic link between photosynthetic electron transport and activation of photosynthetic gene expression.

AB - Activation of the plastid-encoded RNA polymerase is tightly controlled and involves a network of phosphorylation and, as yet unidentified, thiol-mediated events. Here, we characterize PLASTID REDOX INSENSITIVE2, a redox-regulated protein required for full PEP-driven transcription. PRIN2 dimers can be reduced into the active monomeric form by thioredoxins through reduction of a disulfide bond. Exposure to light increases the ratio between the monomeric and dimeric forms of PRIN2. Complementation of prin2-2 with different PRIN2 protein variants demonstrates that the monomer is required for light-activated PEP-dependent transcription and that expression of the nuclear-encoded photosynthesis genes is linked to the activity of PEP. Activation of PEP during chloroplast development likely is the source of a retrograde signal that promotes nuclear LHCB expression. Thus, regulation of PRIN2 is the thiol-mediated mechanism required for full PEP activity, with PRIN2 monomerization via reduction by TRXs providing a mechanistic link between photosynthetic electron transport and activation of photosynthetic gene expression.

UR - http://europepmc.org/articles/PMC5752674

U2 - 10.1038/s41467-017-02468-2

DO - 10.1038/s41467-017-02468-2

M3 - Journal article

C2 - 29298981

VL - 9

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 50

ER -