An Organelle RNA Recognition Motif Protein is Required for Photosynthetic Subunit psbF Transcript Editing

Hackett, Justin; Shi, Xiaowen; Kobylarz, Amy T; Lucas, Meriah K; Wessendorf, Ryan L; Hines, Kevin M; Bentolila, Stéphane; Hanson, Maureen R.; Lu, Yan

doi:10.1104/pp.16.01623

Cited by 33 publications

(58 citation statements)

References 72 publications

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“…Two non-PPR factors are involved in editing of psbF-26 in Arabidopsis: MORF8/RIP1 (Bentolila et al, 2012) and ORRM6 (Hackett et al, 2017). Although their role in the editing reaction is not yet fully understood, disruption of each of these two genes is sufficient to completely abolish editing at psbF-26.…”

Section: Discussionmentioning

confidence: 99%

Establishment of a Heterologous RNA Editing Event in Chloroplasts

et al. 2019

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ORCID IDs: 0000-0001-8210-1216 (F.V.L.); 0000-0003-3210-0260 (M.A.S.); 0000-0001-7502-6940 (R.B.).In chloroplasts and plant mitochondria, specific cytidines in mRNAs are posttranscriptionally converted to uridines by RNA editing. Editing sites are recognized by nucleus-encoded RNA-binding proteins of the pentatricopeptide repeat (PPR) family, which bind upstream of the editing site in a sequence-specific manner and direct the editing activity to the target position. Editing sites have been lost many times during evolution by C-to-T mutations. Loss of an editing site is thought to be accompanied by loss or degeneration of its cognate PPR protein. Consequently, foreign editing sites are usually not recognized when introduced into species lacking the site. Previously, the spinach (Spinacia oleracea) psbF-26 editing site was introduced into the tobacco (Nicotiana tabacum) plastid genome. Tobacco lacks the psbF-26 site and cannot edit it. Expression of the "unedited" PsbF protein resulted in impaired PSII function. In Arabidopsis (Arabidopsis thaliana), the PPR protein LPA66 is required for editing at psbF-26. Here, we show that introduction of the Arabidopsis LPA66 reconstitutes editing of the spinach psbF-26 site in tobacco and restores a wild-type-like phenotype. Our findings define the minimum requirements for establishing new RNA editing sites and suggest that the evolutionary dynamics of editing patterns is largely explained by coevolution of editing sites and PPR proteins.

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Section: Discussionmentioning

confidence: 99%

Establishment of a Heterologous RNA Editing Event in Chloroplasts

et al. 2019

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“…Some organelle‐localized RRM proteins have multiple functions. For instance, both RNA editing and plant development were impaired in the orrm6 mutant …”

Section: Functional Diversity Of Organelle‐localized Rrm Proteinsmentioning

confidence: 99%

“…Subsequently ORRM6, whose RRM exhibits the highest sequence similarity to that in ORRM1 (Figure ), was identified as a factor required for efficient editing of chloroplast sites accD C794 and psbF C77 . ORRM2, 3, 4, and 5 were recently characterized as mitochondrial RNA editing factors, as knockdown or knockout of each gene expression leads to editing defects at 6, 19, 44, and 17% mitochondrial C targets, respectively . Unlike other ORRM editing factors whose absence causes decrease of editing efficiency, absence of ORRM5 in orrm5 mutant plants results in an increase of editing extent in 14% of the mitochondrial sites surveyed …”

Section: Functional Diversity Of Organelle‐localized Rrm Proteinsmentioning

confidence: 99%

“…ORRM1 interacts with the PPR proteins that are required for editing of the same site as ORRM1 . ORRM6 interacts with RIP1, RIP2, RIP9, OZ1, and with itself . However, ORRM6 does not interact with RARE1 or LPA66 (affecting editing at accD C794 and psbF C77, respectively), possibly due to a lack of a RIP motif, which is responsible for ORRM1 interactions with PPR proteins .…”

Section: Functional Diversity Of Organelle‐localized Rrm Proteinsmentioning

confidence: 99%

“…ORRM6 interacts with RIP1, RIP2, RIP9, OZ1, and with itself . However, ORRM6 does not interact with RARE1 or LPA66 (affecting editing at accD C794 and psbF C77, respectively), possibly due to a lack of a RIP motif, which is responsible for ORRM1 interactions with PPR proteins . ORRM3 and ORRM4 interact with RIP1; ORRM3 and ORRM4 form heterodimers with each other and form homodimers with themselves .…”

Section: Functional Diversity Of Organelle‐localized Rrm Proteinsmentioning

confidence: 99%

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Functional diversity of Arabidopsis organelle‐localized RNA‐recognition motif‐containing proteins

2017

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RNA-Binding Proteins (RBPs) play key roles in plant gene expression and regulation. RBPs contain a variety of RNA-binding motifs, the most abundant and most widespread one in eukaryotes is the RNA recognition motif (RRM). Many nucleus-encoded RRM-containing proteins are transported into chloroplasts and/or mitochondria, and participate in various RNA-related processes in plant organelles. Loss of these proteins can have a detrimental effect on some critical processes such as photosynthesis and respiration, sometimes leading to lethality. Progress has been made in the last few years in understanding the function of particular organelle-localized RRM-containing proteins. Members of the Organelle RRM protein (ORRM, some also characterized as Glycine-Rich RNA-Binding Proteins) family and the Chloroplast RiboNucleoProtein (cpRNP) family, are involved in various types of RNA metabolism, including RNA editing, RNA stability and RNA processing. Organelle-localized RRM proteins also function in plant development and stress responses, in some conditions acting as protein or RNA chaperones. There has been recent progress in characterizing the function of organelle-localized RRM proteins in RNA-related processes and how RRM proteins contribute to the normal growth and development of plants. WIREs RNA 2017, 8:e1420. doi: 10.1002/wrna.1420 For further resources related to this article, please visit the WIREs website.

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Two organelle RNA recognition motif proteins affect distinct sets of RNA editing sites in the Arabidopsis thaliana plastid

et al. 2020

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Plastid and mitochondrial RNAs in vascular plants are subjected to cytidine-touridine editing. The model plant species Arabidopsis thaliana (Arabidopsis) has two nuclear-encoded plastid-targeted organelle RNA recognition motif (ORRM) proteins: ORRM1 and ORRM6. In the orrm1 mutant, 21 plastid RNA editing sites were affected but none are essential to photosynthesis. In the orrm6 mutants, two plastid RNA editing sites were affected: psbF-C77 and accD-C794. Because psbF encodes the β subunit of cytochrome b 559 in photosystem II, which is essential to photosynthesis, the orrm6 mutants were much smaller than the wild type. In addition, the orrm6 mutants had pale green leaves and reduced photosynthetic efficiency. To investigate the functional relationship between ORRM1 and ORRM6, we generated orrm1 orrm6 double homozygous mutants. Morphological and physiological analyses showed that the orrm1 orrm6 double mutants had a smaller plant size, reduced chlorophyll contents, and decreased photosynthetic efficiency, similar to the orrm6 single mutants.Although the orrm1 orrm6 double mutants adopted the phenotype of the orrm6 single mutants, the total number of plastid RNA editing sites affected in the orrm1 orrm6 double mutants was the sum of the sites affected in the orrm1 and orrm6 single mutants. These data suggest that ORRM1 and ORRM6 are in charge of distinct sets of plastid RNA editing sites and that simultaneous mutations in ORRM1 and ORRM6 genes do not cause additional reduction in editing extent at other plastid RNA editing sites. K E Y W O R D S multiple organellar RNA editing factors, organelle RNA recognition motif proteins, organelle zinc finger proteins, pentatricopeptide repeat proteins, plastid RNA editing, RNA editing interacting proteins 2 |

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An Organelle RNA Recognition Motif Protein is Required for Photosynthetic Subunit psbF Transcript Editing

Cited by 33 publications

References 72 publications

Establishment of a Heterologous RNA Editing Event in Chloroplasts

Establishment of a Heterologous RNA Editing Event in Chloroplasts

Functional diversity of Arabidopsis organelle‐localized RNA‐recognition motif‐containing proteins

Two organelle RNA recognition motif proteins affect distinct sets of RNA editing sites in the Arabidopsis thaliana plastid

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