<i>Arabidopsis</i>Chromatin Remodeling Factor PICKLE Interacts with Transcription Factor HY5 to Regulate Hypocotyl Cell Elongation

Jing, Yanjun; Zhang, Dong; Wang, Xin; Tang, Weijiang; Wang, Wanqing; Huai, Junling; Xu, Gang; Chen, Dongqin; Li, Yunliang; Lin, Rongcheng

doi:10.1105/tpc.112.105742

Cited by 149 publications

(197 citation statements)

References 70 publications

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“…Plasmids containing N-and C-terminal fusions of YFP were cotransformed into Arabidopsis protoplasts as previously described (38). The protoplasts were then incubated under light for 12-16 h, and the YFP fluorescence was determined using a confocal microscope (Olympus).…”

Section: Methodsmentioning

confidence: 99%

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Tetrapyrrole biosynthetic enzyme protoporphyrinogen IX oxidase 1 is required for plastid RNA editing

Zhang

Tang

Hedtke

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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120

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RNA editing is a posttranscriptional process that covalently alters the sequence of RNA molecules and plays important biological roles in both animals and land plants. In flowering plants, RNA editing converts specific cytidine residues to uridine in both plastid and mitochondrial transcripts. Previous studies identified pentatricopeptide repeat (PPR) motif-containing proteins as site-specific recognition factors for cytidine targets in RNA sequences. However, the regulatory mechanism underlying RNA editing was largely unknown. Here, we report that protoporphyrinogen IX oxidase 1 (PPO1), an enzyme that catalyzes protoporphyrinogen IX into protoporphyrin IX in the tetrapyrrole biosynthetic pathway, plays an unexpected role in editing multiple sites of plastid RNA transcripts, most of which encode subunits of the NADH dehydrogenase-like complex (NDH), in the reference plant Arabidopsis thaliana. We identified multiple organellar RNA editing factors (MORFs), including MORF2, MORF8, and MORF9, that interact with PPO1. We found that two conserved motifs within the 22-aa region at the N terminus of PPO1 are essential for its interaction with MORFs, its RNA editing function, and subsequently, its effect on NDH activity. However, transgenic plants lacking key domains for the tetrapyrrole biosynthetic activity of PPO1 exhibit normal RNA editing. Furthermore, MORF2 and MORF9 interact with three PPRs or related proteins required for editing of ndhB and ndhD sites. These results reveal that the tetrapyrrole biosynthetic enzyme PPO1 is required for plastid RNA editing, acting as a regulator that promotes the stability of MORF proteins through physical interaction. metabolism | organelle | editosome R NA editing, the process of covalently altering the sequence of an RNA molecule, generates protein diversity in eukaryotes (1, 2). Generally, in land plants, RNA editing highly specifically converts cytidine to uridine nucleotides in transcripts of both plastid and mitochondrial genes (3); 34 cytidine residues in plastids and more than 500 residues in mitochondria have been reported to be editing target sites in Arabidopsis thaliana (4, 5). A series of studies identified members of the PLS subfamily of pentatricopeptide repeat (PPR) motif-containing proteins as the site-specific recognition factors for cytidine targets (6). These specific PPR trans-acting proteins recognize cis elements within a region of ∼30 nt within the sites to be edited (1, 6-11). Although the DYW domains of some PPR factors contain several conserved residues with a cytidine deaminase motif (12), the enzyme that executes the editing reaction is elusive. Two recent reports documented that members of multiple organellar RNA editing factors (MORFs)/RNA editing factor interacting proteins (RIPs) widely affect RNA editing sites in both mitochondria and plastids (13,14). Organelle RNA recognition motif protein 1, which contains two truncated RIP domains, is also essential for plastid RNA editing (15). These studies reveal additional components of the plant organel...

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Section: Methodsmentioning

confidence: 99%

“…The procedures used for coimmunoprecipitation and immunoblot assays were described previously (38). Proteins were separated on a 10% (vol/vol) SDS/PAGE gel and detected by immunoblotting with anti-GFP (Abcam) and anti-HA (Invitrogen) antibodies.…”

Section: Methodsmentioning

confidence: 99%

Tetrapyrrole biosynthetic enzyme protoporphyrinogen IX oxidase 1 is required for plastid RNA editing

Zhang

Tang

Hedtke

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

120

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“…Combinatorial regulation exerted by the interaction of other transcription factors with HY5/HYH is widely present, with negative or positive regulatory effects (Shin et al, 2007;Andronis et al, 2008;Holtan et al, 2011;Huang et al, 2012;Jiang et al, 2012;Singh et al, 2012;Gangappa et al, 2013aGangappa et al, , 2013bJing et al, 2013;Abbas et al, 2014). Moreover, HY5 interacts with the chromatin-remodeling factor PICKLE (PKL), recruiting PKL to promoters of target genes repressing the H3K27me3-repressive histone mark (Jing et al, 2013). Thus, an exact understanding of HY5/HYH function in response to UV-B will also require systematic analysis of known HY5-interacting transcriptional regulators and an unbiased approach to identify those that are specifically involved.…”

Section: Regulation Of the Hy5 Association With Chromatinmentioning

confidence: 99%

UV-B-Responsive Association of the Arabidopsis bZIP Transcription Factor ELONGATED HYPOCOTYL5 with Target Genes, Including Its Own Promoter

et al. 2014

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In plants subjected to UV-B radiation, responses are activated that minimize damage caused by UV-B. The bZIP transcription factor ELONGATED HYPOCOTYL5 (HY5) acts downstream of the UV-B photoreceptor UV RESISTANCE LOCUS8 (UVR8) and promotes UV-B-induced photomorphogenesis and acclimation. Expression of HY5 is induced by UV-B; however, the transcription factor(s) that regulate HY5 transcription in response to UV-B and the impact of UV-B on the association of HY5 with its target promoters are currently unclear. Here, we show that HY5 binding to the promoters of UV-B-responsive genes is enhanced by UV-B in a UVR8-dependent manner in Arabidopsis thaliana. In agreement, overexpression of REPRESSOR OF UV-B PHOTOMORPHOGENESIS2, a negative regulator of UVR8 function, blocks UV-B-responsive HY5 enrichment at target promoters. Moreover, we have identified a T/G-box in the HY5 promoter that is required for its UV-B responsiveness. We show that HY5 and its homolog HYH bind to the T/G HY5 -box cis-acting element and that they act redundantly in the induction of HY5 expression upon UV-B exposure. Therefore, HY5 is enriched at target promoters in response to UV-B in a UVR8 photoreceptor-dependent manner, and HY5 and HYH interact directly with a T/G-box cis-acting element of the HY5 promoter, mediating the transcriptional activation of HY5 in response to UV-B.

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“…Anti-GST (Abcam), anti-His (Abcam), anti-Myc (Abcam), and anti-D1 (Agrisera) were commercially available. Anti-HY5 and antitubulin antibodies were raised in rabbits (Jing et al, 2013).…”

Section: Emsamentioning

confidence: 99%

Antagonistic Basic Helix-Loop-Helix/bZIP Transcription Factors Form Transcriptional Modules That Integrate Light and Reactive Oxygen Species Signaling inArabidopsis

et al. 2013

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The critical developmental switch from heterotrophic to autotrophic growth of plants involves light signaling transduction and the production of reactive oxygen species (ROS). ROS function as signaling molecules that regulate multiple developmental processes, including cell death. However, the relationship between light and ROS signaling remains unclear. Here, we identify transcriptional modules composed of the basic helix-loop-helix and bZIP transcription factors PHYTOCHROME-INTERACTING FACTOR1 (PIF1), PIF3, ELONGATED HYPOCOTYL5 (HY5), and HY5 HOMOLOGY (HYH) that bridge light and ROS signaling to regulate cell death and photooxidative response. We show that pif mutants release more singlet oxygen and exhibit more extensive cell death than the wild type during Arabidopsis thaliana deetiolation. Genome-wide expression profiling indicates that PIF1 represses numerous ROS and stress-related genes. Molecular and biochemical analyses reveal that PIF1/PIF3 and HY5/HYH physically interact and coordinately regulate the expression of five ROS-responsive genes by directly binding to their promoters. Furthermore, PIF1/PIF3 and HY5/HYH function antagonistically during the seedling greening process. In addition, phytochromes, cryptochromes, and CONSTITUTIVE PHOTOMORPHOGENIC1 act upstream to regulate ROS signaling. Together, this study reveals that the PIF1/PIF3-HY5/HYH transcriptional modules mediate crosstalk between light and ROS signaling and sheds light on a new mechanism by which plants adapt to the light environments.

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ArabidopsisChromatin Remodeling Factor PICKLE Interacts with Transcription Factor HY5 to Regulate Hypocotyl Cell Elongation

Cited by 149 publications

References 70 publications

Tetrapyrrole biosynthetic enzyme protoporphyrinogen IX oxidase 1 is required for plastid RNA editing

Tetrapyrrole biosynthetic enzyme protoporphyrinogen IX oxidase 1 is required for plastid RNA editing

UV-B-Responsive Association of the Arabidopsis bZIP Transcription Factor ELONGATED HYPOCOTYL5 with Target Genes, Including Its Own Promoter

Antagonistic Basic Helix-Loop-Helix/bZIP Transcription Factors Form Transcriptional Modules That Integrate Light and Reactive Oxygen Species Signaling inArabidopsis

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