Plastid transformation reveals that moss tRNA<sup>Arg</sup>‐CCG is not essential for plastid function

Sugiura, Chika; Sugita, Mamoru

doi:10.1111/j.1365-313x.2004.02202.x

Cited by 52 publications

(36 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ACG to ICG modification of the anticodon is believed to be required to read all four CGN codons for arginine (Pfitzinger et al 1990;Sugiura and Sugita 2004). The tRNA with the unmodified anticodon should not be suitable to decode CGA and CGG triplets (Crick 1966).…”

Section: Phenotype Of Attada Rnai Linesmentioning

confidence: 99%

Identification of the chloroplast adenosine-to-inosine tRNA editing enzyme

Karcher¹,

Bock²

2009

RNA

View full text Add to dashboard Cite

Plastids (chloroplasts) of higher plants exhibit two types of conversional RNA editing: cytidine-to-uridine editing in mRNAs and adenosine-to-inosine editing in at least one plastid genome-encoded tRNA, the tRNA-Arg(ACG). The enzymes catalyzing RNA editing reactions in plastids are unknown. Here we report the identification of the A-to-I tRNA editing enzyme from chloroplasts of the model plant Arabidopsis thaliana. The protein (AtTadA) has an unusual structure in that it harbors a large N-terminal domain of >1000 amino acids, which is not required for catalytic activity. The C-terminal region of the protein displays sequence similarity to tadA, the tRNA adenosine deaminase from Escherichia coli. We show that AtTadA is imported into chloroplasts in vivo and demonstrate that the in vitro translated protein triggers A-to-I editing in the anticodon of the plastid tRNA-Arg(ACG). Suppression of AtTadA gene expression in transgenic Arabidopsis plants by RNAi results in reduced A-to-I editing in the chloroplast tRNA-Arg(ACG). The RNAi lines display a mild growth phenotype, presumably due to reduced chloroplast translational efficiency upon limited availability of edited tRNA-Arg(ACG).

show abstract

Section: Phenotype Of Attada Rnai Linesmentioning

confidence: 99%

Identification of the chloroplast adenosine-to-inosine tRNA editing enzyme

Karcher¹,

Bock²

2009

RNA

View full text Add to dashboard Cite

show abstract

“…The genome sequences are known for the chloroplast (20), the mitochondrion (21), and the nucleus (22). Gene targeting is feasible in the nuclear and chloroplast genomes (23,24). Furthermore, the P. patens gametophyte, the haploid phase of the life cycle, is dominant, making it possible to study the phenotypes of knockouts directly without further crosses.…”

mentioning

confidence: 99%

A Pentatricopeptide Repeat Protein Is Required for RNA Processing of clpP Pre-mRNA in Moss Chloroplasts

Hattori

Miyake

Sugita

2007

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Pentatricopeptide repeat (PPR) proteins are encoded by the nuclear genome as a large gene family in land plants. PPR proteins play essential roles in organelle-related functions, mostly in RNA-processing steps in plastids and mitochondria. In the moss Physcomitrella patens, there is also a large gene family, but the moss PPR proteins are likely to be divergent from those of higher plants. To investigate the function of plastid PPR proteins, we have generated and characterized a PPR protein gene disruptant of P. patens. The PPR531-11-disrupted mosses displayed abnormal phenotypic characteristics, such as a significantly smaller protonemal colony, different chloroplast morphology, and incomplete thylakoid membrane formation. In addition, the quantum yield of photosystem II was reduced in the disrupted mosses. To further investigate whether disruption of the PPR531-11 gene affects chloroplast gene expression, we performed Northern blot and reverse transcription polymerase chain reaction analyses. These analyses revealed that PPR531-11 has a role in intergenic RNA cleavage between clpP and 5-rps12 and in the splicing of clpP pre-mRNA. Western blot analysis showed that disruption of PPR531-11 resulted in a reduced level of ClpP, photosystem II reaction center protein D1, and the stromal enzyme, ribulose-bisphosphate carboxylase/oxygenase. These reductions might result in the severely retarded growth of the protonemal colony. Taken together, we propose a model where PPR531-11 function affects the steadystate level of ClpP, which regulates the formation and maintenance of thylakoid membranes in chloroplasts. This is the first evidence of a PPR protein controlling the protein expression level of ClpP. The pentatricopeptide repeat (PPR)2 is a degenerate 35-amino acid repeating motif that is found in animals, fungi, and plants (1). The PPR motif is similar to but distinct from the tetratricopeptide repeat motif, a well characterized protein interaction motif that is composed of 34 amino acids (2). A particularly large gene family encoding PPR proteins exists in plants, from mosses (3) to flowering plants (4), but not in fungi and animals. For instance, the Arabidopsis thaliana and the rice (Oryza sativa) genomes encode more than 400 PPR proteins. Most plant PPR proteins are predicted to be targeted to the mitochondria or chloroplasts (4). Many PPR proteins play important roles in a wide range of physiological and developmental functions, i.e. cytoplasmic male sterility (5, 6), fertility restoration (7), photosynthesis (8, 9), chloroplast biogenesis (10), and early or late embryogenesis (11,12).Many chloroplast genes of land plants are cotranscribed as polycistronic pre-RNAs, which are then extensively processed into shorter mature RNA species (13). Recently, several lines of evidence that PPR proteins are involved in post-transcriptional regulation in chloroplast gene expression have accumulated. For instance, the maize PPR protein CRP1 is required for intergenic RNA processing of petB and petD dicistronic mRNA (8). The m...

show abstract

“…In fact, homologous recombination has been observed in a chloroplast genome. [1][2][3] Homologous recombination is a process that occurs in all organisms. It is responsible for genetic diversity, the maintenance of genome integrity, and the proper segregation of chromosomes.…”

mentioning

confidence: 99%

Expression and Complementation Analyses of a Chloroplast-Localized Homolog of Bacterial RecA in the MossPhyscomitrella patens

Inouye

Odahara

Fujita

et al. 2008

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Plastid transformation reveals that moss tRNA^Arg‐CCG is not essential for plastid function

Cited by 52 publications

References 38 publications

Identification of the chloroplast adenosine-to-inosine tRNA editing enzyme

Identification of the chloroplast adenosine-to-inosine tRNA editing enzyme

A Pentatricopeptide Repeat Protein Is Required for RNA Processing of clpP Pre-mRNA in Moss Chloroplasts

Expression and Complementation Analyses of a Chloroplast-Localized Homolog of Bacterial RecA in the MossPhyscomitrella patens

Contact Info

Product

Resources

About

Plastid transformation reveals that moss tRNAArg‐CCG is not essential for plastid function

Cited by 52 publications

References 38 publications

Identification of the chloroplast adenosine-to-inosine tRNA editing enzyme

Identification of the chloroplast adenosine-to-inosine tRNA editing enzyme

A Pentatricopeptide Repeat Protein Is Required for RNA Processing of clpP Pre-mRNA in Moss Chloroplasts

Expression and Complementation Analyses of a Chloroplast-Localized Homolog of Bacterial RecA in the MossPhyscomitrella patens

Contact Info

Product

Resources

About

Plastid transformation reveals that moss tRNA^Arg‐CCG is not essential for plastid function