Chloroplast RNA-binding proteins: Repair and regulation of chloroplast transcripts

Tillich, Michael; Beick, Susanne; Schmitz‐Linneweber, Christian

doi:10.4161/rna.7.2.11090

Cited by 28 publications

(27 citation statements)

References 68 publications

(88 reference statements)

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“…In contrast, the cpRNPs (and possibly other RRM proteins) are highly expressed, seem to act on multiple RNAs, react rapidly to various stresses and developmental signals, and are important for RNA turnover. Hypothetically, the cpRNPs seem to work like their nucleo-cytosolic counterparts (the hnRNPs) in helping to co-regulate large sets of mRNAs (Tillich et al, 2010). Their co-expression with photosynthetic genes in the chloroplast and nucleus supports this notion.…”

Section: Discussionmentioning

confidence: 86%

The RNA-recognition motif in chloroplasts

Ruwe

Kupsch

Teubner

et al. 2011

Journal of Plant Physiology

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Section: Discussionmentioning

confidence: 86%

The RNA-recognition motif in chloroplasts

Ruwe

Kupsch

Teubner

et al. 2011

Journal of Plant Physiology

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“…This implies that they are resistant to ribonucleases, despite the fact that they lack both a 5′-triphosphate and stable structure, the two intrinsic features that are predicted to be protective (1,17,40). It seems, therefore, that sRNAs lacking such protective features must be protected by bound proteins.Chloroplasts house an abundance of RNA binding proteins with various types of RNA binding domains (1,41). We suggest, however, that it is the PPR class (and PPR-like proteins with long tracts of other repeating units) that is primarily responsible for stabilizing sRNAs and corresponding processed mRNA termini.…”

Section: Discussionmentioning

confidence: 99%

Protein-mediated protection as the predominant mechanism for defining processed mRNA termini in land plant chloroplasts

Zhelyazkova

Hammani

Rojas

et al. 2011

Nucleic Acids Research

121

202

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Most chloroplast mRNAs are processed from larger precursors. Several mechanisms have been proposed to mediate these processing events, including site-specific cleavage and the stalling of exonucleases by RNA structures. A protein barrier mechanism was proposed based on analysis of the pentatricopeptide repeat (PPR) protein PPR10: PPR10 binds two intercistronic regions and impedes 5′- and 3′-exonucleases, resulting in processed RNAs with PPR10 bound at the 5′- or 3′-end. In this study, we provide evidence that protein barriers are the predominant means for defining processed mRNA termini in chloroplasts. First, we map additional RNA termini whose arrangement suggests biogenesis via a PPR10-like mechanism. Second, we show that the PPR protein HCF152 binds to the immediate 5′- or 3′-termini of transcripts that require HCF152 for their accumulation, providing evidence that HCF152 defines RNA termini by blocking exonucleases. Finally, we build on the observation that the PPR10 and HCF152 binding sites accumulate as small chloroplast RNAs to infer binding sites of other PPR proteins. We show that most processed mRNA termini are represented by small RNAs whose sequences are highly conserved. We suggest that each such small RNA is the footprint of a PPR-like protein that protects the adjacent RNA from degradation.

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“…Although expression of several chloroplast RNA binding proteins was shown to depend on development, tissues, and environmental conditions, a truly regulatory function has been shown, to the best of our knowledge, only for the PPR protein MCA1, a factor in C. reinhardtii (Raynaud et al, 2007;Tillich et al, 2010;Ruwe et al, 2011). It appeared that the abundance of MCA1 limits the amount of petA mRNA and accordingly levels of the encoded protein, cytochrome f (Raynaud et al, 2007).…”

Section: Prfb3 Expression Is Highly Responsive To Stress and Environmmentioning

confidence: 99%

Recruitment of a Ribosomal Release Factor for Light- and Stress-Dependent Regulation of petB Transcript Stability in Arabidopsis Chloroplasts

Stoppel¹,

Lezhneva²,

Schwenkert³

et al. 2011

Plant Cell

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Land plant genomes encode four functional ribosomal peptide chain release factors (Prf) of eubacterial origin, two (PrfA and PrfB homologs) for each endosymbiotic organelle. Formerly, we have shown that the Arabidopsis thaliana chloroplastlocalized PrfB homolog, PrfB1, is required not only for termination of translation but also for stabilization of UGA stop codon-containing chloroplast transcripts. A previously undiscovered PrfB-like protein, PrfB3, is localized to the chloroplast stroma in a petB RNA-containing complex and found only in vascular plants. Highly conserved positions of introns unequivocally indicate that PrfB3 arose from a duplication of PrfB1. Notably, PrfB3 is lacking the two most important tripeptide motifs characteristic for all eubacterial and organellar PrfB homologs described so far: the stop codon recognition motif SPF and the catalytic center GGQ for peptidyl-tRNA hydrolysis. Complementation studies, as well as functional and molecular analyses of two allelic mutations in Arabidopsis, both of which lead to a specific deficiency of the cytochrome b 6 f complex, revealed that PrfB3 is essentially required for photoautotrophic growth. Plastid transcript, polysome, and translation analyses indicate that PrfB3 has been recruited in vascular plants for light-and stress-dependent regulation of stability of 39 processed petB transcripts to adjust cytochrome b 6 levels.

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Chloroplast RNA-binding proteins: Repair and regulation of chloroplast transcripts

Cited by 28 publications

References 68 publications

The RNA-recognition motif in chloroplasts

The RNA-recognition motif in chloroplasts

Protein-mediated protection as the predominant mechanism for defining processed mRNA termini in land plant chloroplasts

Recruitment of a Ribosomal Release Factor for Light- and Stress-Dependent Regulation of petB Transcript Stability in Arabidopsis Chloroplasts

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