Recruitment of a peptidyl-tRNA hydrolase as a facilitator of group II intron splicing in chloroplasts

Jenkins, Bethany D.; Barkan, Alice

doi:10.1093/emboj/20.4.872

Cited by 112 publications

(137 citation statements)

References 26 publications

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“…The other cofactors and RNA splicing factors are encoded by nuclear genes and are imported into organelles. Four of these (CRS1, CRS2, CAF1, and CAF2) that act as factors in splicing of one or more different introns have been identified from maize chloroplasts (Jenkins and Barkan, 2001;Till et al, 2001;Ostheimer et al, 2003Ostheimer et al, , 2005Ostheimer et al, , 2006Ostersetzer et al, 2005), and a PPR protein has been characterized that is specifically needed for trans-splicing of the rps12 transcript (Schmitz-Linneweber et al, 2006). RNA trans-splicing probably requires more proteins than cis-splicing, and many more may remain to be identified in land plants if we compare the currently known factors with the 14 nuclear genes that are required for the removal of the transspliced introns in the psaA gene in Chlamydomonas reinhardtii chloroplasts (Goldschmidt-Clermont et al, 1990;Merendino et al, 2006).…”

Section: Discussion Plant Organellar Splicing Factorsmentioning

confidence: 99%

The Pentatricopeptide Repeat GeneOTP43Is Required fortrans-Splicing of the Mitochondrialnad1Intron 1 inArabidopsis thaliana

et al. 2007

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The mitochondrial NADH:ubiquinone oxidoreductase complex (Complex I) is a large protein complex formed from both nuclearly and mitochondrially encoded subunits. Subunit ND1 is encoded by a mitochondrial gene comprising five exons, and the mature transcript requires four RNA splicing events, two of which involve trans-splicing independently transcribed RNAs. We have identified a nuclear gene (OTP43) absolutely required for trans-splicing of intron 1 (and only intron 1) of Arabidopsis thaliana nad1 transcripts. This gene encodes a previously uncharacterized pentatricopeptide repeat protein.Mutant Arabidopsis plants with a disrupted OTP43 gene do not present detectable mitochondrial Complex I activity and show severe defects in seed development, germination, and to a lesser extent in plant growth. The alternative respiratory pathway involving alternative oxidase is significantly induced in the mutant.

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Section: Discussion Plant Organellar Splicing Factorsmentioning

confidence: 99%

The Pentatricopeptide Repeat GeneOTP43Is Required fortrans-Splicing of the Mitochondrialnad1Intron 1 inArabidopsis thaliana

et al. 2007

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“…The ndhA and ndhB introns are not designated as APO1 ligands because the splicing defects in apo1 mutants were mild. Results are summarized from this work and from previously published work (Jenkins et al, 1997;Vogel et al, 1999;Jenkins and Barkan, 2001;Till et al, 2001;Ostheimer et al, 2003;Schmitz-Linneweber et al, 2006;Asakura and Barkan, 2007;Watkins et al, 2007;Asakura et al, 2008;Beick et al, 2008;de Longevialle et al, 2008;Prikryl et al, 2008;Kroeger et al, 2009). …”

Section: Phylogenetic Analysismentioning

confidence: 99%

“…Ycf3-int2 is the only member of this group whose splicing does not require a heterodimer between the peptidyl-tRNA hydrolase homolog CRS2 and either of two paralogous proteins CAF1 or CAF2 (Jenkins et al, 1997;Jenkins and Barkan, 2001;Ostheimer et al, 2003). It is also the only cis-spliced member of this group that requires neither of the two paralogous proteins CFM2 or CFM3 Asakura et al, 2008).…”

Section: Group II Intron Splicing Factors In Chloroplastsmentioning

confidence: 99%

APO1 Promotes the Splicing of Chloroplast Group II Introns and Harbors a Plant-Specific Zinc-Dependent RNA Binding Domain

et al. 2011

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Arabidopsis thaliana APO1 is required for the accumulation of the chloroplast photosystem I and NADH dehydrogenase complexes and had been proposed to facilitate the incorporation of [4Fe-4S] clusters into these complexes. The identification of maize (Zea mays) APO1 in coimmunoprecipitates with a protein involved in chloroplast RNA splicing prompted us to investigate a role for APO1 in splicing. We show here that APO1 promotes the splicing of several chloroplast group II introns: in Arabidopsis apo1 mutants, ycf3-intron 2 remains completely unspliced, petD intron splicing is strongly reduced, and the splicing of several other introns is compromised. These splicing defects can account for the loss of photosynthetic complexes in apo1 mutants. Recombinant APO1 from both maize and Arabidopsis binds RNA with high affinity in vitro, demonstrating that DUF794, the domain of unknown function that makes up almost the entirety of APO1, is an RNA binding domain. We provide evidence that DUF794 harbors two motifs that resemble zinc fingers, that these bind zinc, and that they are essential for APO1 function. DUF794 is found in a plant-specific protein family whose members are all predicted to localize to mitochondria or chloroplasts. Thus, DUF794 adds a new example to the repertoire of plant-specific RNA binding domains that emerged as a product of nuclear-organellar coevolution.

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“…The first includes RNA-binding proteins derived from enzymes involved in RNA metabolism such as for example pseudouridine synthase (Perron et al, 1999) and peptidyl-tRNA hydrolase (Jenkins and Barkan, 2001). These proteins appear to have been recruited for novel roles in chloroplast gene expression during evolution.…”

Section: Assembly Of Photosynthetic Complexesmentioning

confidence: 99%

Assembly of the Photosynthetic Apparatus

Rochaix

2011

Plant Physiology

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The primary reactions of photosynthesis are mediated by three protein complexes embedded in the thylakoid membranes of chloroplasts. These complexes are PSII, the cytochrome b 6 f complex (Cytb 6 f), and PSI, which are connected in series through the photosynthetic electron transport chain. Light energy captured by the light-harvesting systems of PSII (LHCII) and PSI (LHCI) is transferred to the reaction center chlorophylls to create a charge separation across the membrane. This leads to the formation of a strong oxidant on the donor side of PSII capable of splitting water into molecular oxygen, protons, and electrons. The electrons are transferred stepwise from PSII to the plastoquinone pool, Cytb 6 f, plastocyanin, and PSI where a second charge separation creates a strong reductant capable of reducing ferredoxin that subsequently reduces NADP + to NADPH. Besides this linear electron pathway there is a cyclic pathway in which electrons are cycled around PSI through the Cytb 6 f complex. The electron transfer reactions are coupled to proton pumping into the lumen space of the thylakoids and the resulting pH gradient drives the ATP synthase for ATP production. Ultimately NADPH and ATP are used for CO 2 assimilation by the Calvin-Benson cycle. Thylakoid membranes of land plants are organized in two domains, the grana stacks, comprising 80% of the membrane, and the stromal nonappressed membranes that connect different grana stacks. The photosynthetic complexes with exception of Cytb 6 f, are not distributed evenly through the thylakoid membrane system. Whereas PSII is mostly confined to the grana regions, PSI and ATP synthase are located in the stroma lamellae. Electron transfer between these complexes is mediated by the diffusible electron carriers plastoquinone and plastocyanin.A characteristic feature of the photosynthetic complexes is that they all consist of numerous chloroplast and nucleus-encoded subunits. In the case of PSII, PSI, and Cytb 6 f these complexes contain in addition pigments such as chlorophylls and xanthophylls as well as hemes, quinones, and iron-sulfur (Fe-S) centers that act as redox cofactors. Hence the biogenesis of the photosynthetic apparatus involves a concerted interplay between the chloroplast and nucleocytosolic genetic systems as well as a tight coordination between protein and pigment synthesis and insertion into the thylakoid membranes. Analysis of numerous mutants affected in photosynthetic activity in Chlamydomonas reinhardtii, Arabidopsis (Arabidopsis thaliana), and Zea mays has provided many new insights into the assembly of the photosynthetic complexes (Barkan and Goldschmidt-Clermont, 2000;Eberhard et al., 2008).A remarkable feature of photosynthetic organisms is their ability to adapt to changing light conditions, which is reflected in changes in the organization of the photosynthetic complexes. This Update reviews recent advances in our understanding of the assembly of these complexes and for some of them, their remodeling and/or reversible association into supercomplexes...

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Recruitment of a peptidyl-tRNA hydrolase as a facilitator of group II intron splicing in chloroplasts

Cited by 112 publications

References 26 publications

The Pentatricopeptide Repeat GeneOTP43Is Required fortrans-Splicing of the Mitochondrialnad1Intron 1 inArabidopsis thaliana

The Pentatricopeptide Repeat GeneOTP43Is Required fortrans-Splicing of the Mitochondrialnad1Intron 1 inArabidopsis thaliana

APO1 Promotes the Splicing of Chloroplast Group II Introns and Harbors a Plant-Specific Zinc-Dependent RNA Binding Domain

Assembly of the Photosynthetic Apparatus

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