Localized control of oxidized RNA

Zhan, Yu; Dhaliwal, James; Adjibade, Pauline; Uniacke, James; Mazrouï, Rachid; Zerges, William

doi:10.1242/jcs.175232

Cited by 25 publications

(24 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…5A, Fig. S3), as in lichenized Trebouxia (Candotto Carniel et al, 2015), perhaps related to compartmentalizing oxidized mRNAs in the pyrenoid (Zhan et al, 2015). Fluorescent DCF also accumulated in the periplasmic space in the aquatic, but not the desert, taxa (Fig.…”

Section: Discussionmentioning

confidence: 90%

A model suite of green algae within the Scenedesmaceae for investigating contrasting desiccation tolerance and morphology

Cardon

Peredo

Dohnálková

et al. 2018

Journal of Cell Science

View full text Add to dashboard Cite

Microscopic green algae inhabiting desert microbiotic crusts are remarkably diverse phylogenetically, and many desert lineages have independently evolved from aquatic ancestors. Here we worked with five desert and aquatic species within the family Scenedesmaceae to examine mechanisms that underlie desiccation tolerance and release of unicellular versus multicellular progeny. Live cell staining and time-lapse confocal imaging coupled with transmission electron microscopy established that the desert and aquatic species all divide by multiple (rather than binary) fission, although progeny were unicellular in three species and multicellular (joined in a sheet-like coenobium) in two. During division, Golgi complexes were localized near nuclei, and all species exhibited dynamic rotation of the daughter cell mass within the mother cell wall at cytokinesis. Differential desiccation tolerance across the five species, assessed from photosynthetic efficiency during desiccation/rehydration cycles, was accompanied by differential accumulation of intracellular reactive oxygen species (ROS) detected using a dye sensitive to intracellular ROS. Further comparative investigation will aim to understand the genetic, ultrastructural and physiological characteristics supporting unicellular versus multicellular coenobial morphology, and the ability of representatives in the Scenedesmaceae to colonize ecologically diverse, even extreme, habitats.

show abstract

Section: Discussionmentioning

confidence: 90%

A model suite of green algae within the Scenedesmaceae for investigating contrasting desiccation tolerance and morphology

Cardon

Peredo

Dohnálková

et al. 2018

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…The ΔrbcL mutant carries a disruption of the chloroplast gene encoding RbcL and lacks a pyrenoid [ 24 , 34 ]. Analysis by SDS-PAGE and silver staining revealed that P fractions from ΔrbcL lacked both RbcL and RbcS, which is known to have a very low abundance in RbcL-deficient mutants [ 25 ] ( Fig 1D ). The Rubisco deficiency of ΔrbcL considerably alters cellular metabolism and might therefore alter the non-pyrenoid proteins in the P fraction, thereby biasing the subtraction of contaminants.…”

Section: Resultsmentioning

confidence: 99%

Pyrenoid functions revealed by proteomics in Chlamydomonas reinhardtii

et al. 2018

Self Cite

View full text Add to dashboard Cite

Organelles are intracellular compartments which are themselves compartmentalized. Biogenic and metabolic processes are localized to specialized domains or microcompartments to enhance their efficiency and suppress deleterious side reactions. An example of intra-organellar compartmentalization is the pyrenoid in the chloroplasts of algae and hornworts. This microcompartment enhances the photosynthetic CO2-fixing activity of the Calvin-Benson cycle enzyme Rubisco, suppresses an energetically wasteful oxygenase activity of Rubisco, and mitigates limiting CO2 availability in aquatic environments. Hence, the pyrenoid is functionally analogous to the carboxysomes in cyanobacteria. However, a comprehensive analysis of pyrenoid functions based on its protein composition is lacking. Here we report a proteomic characterization of the pyrenoid in the green alga Chlamydomonas reinhardtii. Pyrenoid-enriched fractions were analyzed by quantitative mass spectrometry. Contaminant proteins were identified by parallel analyses of pyrenoid-deficient mutants. This pyrenoid proteome contains 190 proteins, many of which function in processes that are known or proposed to occur in pyrenoids: e.g. the carbon concentrating mechanism, starch metabolism or RNA metabolism and translation. Using radioisotope pulse labeling experiments, we show that pyrenoid-associated ribosomes could be engaged in the localized synthesis of the large subunit of Rubisco. New pyrenoid functions are supported by proteins in tetrapyrrole and chlorophyll synthesis, carotenoid metabolism or amino acid metabolism. Hence, our results support the long-standing hypothesis that the pyrenoid is a hub for metabolism. The 81 proteins of unknown function reveal candidates for new participants in these processes. Our results provide biochemical evidence of pyrenoid functions and a resource for future research on pyrenoids and their use to enhance agricultural plant productivity. Data are available via ProteomeXchange with identifier PXD004509.

show abstract

“…The phylogenetic conservation of the DLA2 amino acid sequence and RNA binding properties suggests that it performs a similar dual function in seed plants (Bohne et al, 2013). A moonlighting function was also suggested for RbcL, which was shown to bind RNA (Yosef et al, 2004;Cohen et al, 2006) and recently has been proposed to be involved in the redox stress-induced localization of oxidized chloroplast RNAs in Chlamydomonas, independent of its function in the Rubisco complex (Zhan et al, 2015). Moreover, recent in vitro data suggest that PsbD protein synthesis in Chlamydomonas is metabolically controlled (Schwarz et al, 2012;see above).…”

Section: Translational Regulation In Response To Other Internal and Ementioning

confidence: 96%

Chloroplast Translation: Structural and Functional Organization, Operational Control, and Regulation

2018

View full text Add to dashboard Cite

Chloroplast translation is essential for cellular viability and plant development. Its positioning at the intersection of organellar RNA and protein metabolism makes it a unique point for the regulation of gene expression in response to internal and external cues. Recently obtained high-resolution structures of plastid ribosomes, the development of approaches allowing genome-wide analyses of chloroplast translation (i.e., ribosome profiling), and the discovery of RNA binding proteins involved in the control of translational activity have greatly increased our understanding of the chloroplast translation process and its regulation. In this review, we provide an overview of the current knowledge of the chloroplast translation machinery, its structure, organization, and function. In addition, we summarize the techniques that are currently available to study chloroplast translation and describe how translational activity is controlled and which -elements and-factors are involved. Finally, we discuss how translational control contributes to the regulation of chloroplast gene expression in response to developmental, environmental, and physiological cues. We also illustrate the commonalities and the differences between the chloroplast and bacterial translation machineries and the mechanisms of protein biosynthesis in these two prokaryotic systems.

show abstract

Localized control of oxidized RNA

Cited by 25 publications

References 49 publications

A model suite of green algae within the Scenedesmaceae for investigating contrasting desiccation tolerance and morphology

A model suite of green algae within the Scenedesmaceae for investigating contrasting desiccation tolerance and morphology

Pyrenoid functions revealed by proteomics in Chlamydomonas reinhardtii

Chloroplast Translation: Structural and Functional Organization, Operational Control, and Regulation

Contact Info

Product

Resources

About