Chloroplast-localized translation for protein targeting in <i>Chlamydomonas reinhardtii</i>

Sun, Yuena; Bakhtiari, Shiva; Valente-Paterno, Melissa; Wu, Yanxia; Law, Chris; Dai, Daniel; Dhaliwal, James; Bui, Khanh Huy; Zerges, William

doi:10.1101/2021.12.27.474283

Cited by 4 publications

(5 citation statements)

References 44 publications

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“…That polypeptides are delivered by cotranslational translocation to the endoplasmic reticulum (ER) and mitochondria from ribosomes bound at their outer surfaces (20,149) is well established. Similarly, recent studies in the unicellular alga Chlamydomonas suggest that a domain of the chloroplast outer envelope membrane is bound by ribosomes translating messenger RNAs for chloroplast preproteins (131,142) (Figure 1; Table 1).…”

Section: Protein Targeting To the Chloroplast Surfacementioning

confidence: 59%

Chloroplast Proteostasis: Import, Sorting, Ubiquitination, and Proteolysis

Sun

Jarvis

2023

Annu. Rev. Plant Biol.

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Chloroplasts are the defining plant organelles with responsibility for photosynthesis and other vital functions. To deliver these functions, they possess a complex proteome comprising thousands of largely nucleus-encoded proteins. Composition of the proteome is controlled by diverse processes affecting protein translocation and degradation—our focus here. Most chloroplast proteins are imported from the cytosol via multiprotein translocons in the outer and inner envelope membranes (the TOC and TIC complexes, respectively), or via one of several noncanonical pathways, and then sorted by different systems to organellar subcompartments. Chloroplast proteolysis is equally complex, involving the concerted action of internal proteases of prokaryotic origin and the nucleocytosolic ubiquitin–proteasome system (UPS). The UPS degrades unimported proteins in the cytosol and chloroplast-resident proteins via chloroplast-associated protein degradation (CHLORAD). The latter targets the TOC apparatus to regulate protein import, as well as numerous internal proteins directly, to reconfigure chloroplast functions in response to developmental and environmental signals. Expected final online publication date for the Annual Review of Plant Biology, Volume 74 is May 2023. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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Section: Protein Targeting To the Chloroplast Surfacementioning

confidence: 59%

Chloroplast Proteostasis: Import, Sorting, Ubiquitination, and Proteolysis

Sun

Jarvis

2023

Annu. Rev. Plant Biol.

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“…Chloroplast protein transport is facilitated by the translocon of the outer membrane (TOC) and translocon of the inner membrane (TIC) protein complexes [ 58 , 59 , 60 , 61 ] ( Figure 1 ). Interestingly, the TOC and TIC complexes spatially align with the T-zone suggesting a highly coordinated system of protein import and translation in the Chlamydomonas chloroplast [ 62 , 63 , 64 ].…”

Section: Discussionmentioning

confidence: 99%

“…Chloroplast protein transport is facilitated by the translocon of the outer membrane (TOC) and translocon of the inner membrane (TIC) protein complexes [58][59][60][61] (Figure 1). Interestingly, the TOC and TIC complexes spatially align with the T-zone suggesting a highly coordinated system of protein import and translation in the Chlamydomonas chloroplast [62][63][64]. Nuclear-encoded chloroplast proteins (including Chlamydomonas PSII subunits PsbO, PsbP, PsbQ [52], PsbW [53], and PsbX [54] (Figure 2)), are translated in the cytosol [55], targeted to the chloroplast [56], and then imported across the outer and inner chloroplast membranes using energy from ATP hydrolysis [57].…”

Section: Architecture Of the Chlamydomonas Chloroplastmentioning

confidence: 99%

Assembly and Repair of Photosystem II in Chlamydomonas reinhardtii

Mehra,

Wang,

Russell

et al. 2024

Plants

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Oxygenic photosynthetic organisms use Photosystem II (PSII) to oxidize water and reduce plastoquinone. Here, we review the mechanisms by which PSII is assembled and turned over in the model green alga Chlamydomonas reinhardtii. This species has been used to make key discoveries in PSII research due to its metabolic flexibility and amenability to genetic approaches. PSII subunits originate from both nuclear and chloroplastic gene products in Chlamydomonas. Nuclear-encoded PSII subunits are transported into the chloroplast and chloroplast-encoded PSII subunits are translated by a coordinated mechanism. Active PSII dimers are built from discrete reaction center complexes in a process facilitated by assembly factors. The phosphorylation of core subunits affects supercomplex formation and localization within the thylakoid network. Proteolysis primarily targets the D1 subunit, which when replaced, allows PSII to be reactivated and completes a repair cycle. While PSII has been extensively studied using Chlamydomonas as a model species, important questions remain about its assembly and repair which are presented here.

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“…These mostly encode subunits of the photosynthetic apparatus and components of the chloroplast transcriptiontranslation machinery, including the single, plastid-encoded RNA polymerase (PEP) [15]. Nuclear gene expression is thus responsible for the synthesis of most plastid proteins (≈3000) [16], which are imported into the organelle as precursors [17,18].…”

Section: Chloroplast Genetics In a Nutshellmentioning

confidence: 99%

Harnessing the Algal Chloroplast for Heterologous Protein Production

et al. 2022

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Photosynthetic microbes are gaining increasing attention as heterologous hosts for the light-driven, low-cost production of high-value recombinant proteins. Recent advances in the manipulation of unicellular algal genomes offer the opportunity to establish engineered strains as safe and viable alternatives to conventional heterotrophic expression systems, including for their use in the feed, food, and biopharmaceutical industries. Due to the relatively small size of their genomes, algal chloroplasts are excellent targets for synthetic biology approaches, and are convenient subcellular sites for the compartmentalized accumulation and storage of products. Different classes of recombinant proteins, including enzymes and peptides with therapeutical applications, have been successfully expressed in the plastid of the model organism Chlamydomonas reinhardtii, and of a few other species, highlighting the emerging potential of transplastomic algal biotechnology. In this review, we provide a unified view on the state-of-the-art tools that are available to introduce protein-encoding transgenes in microalgal plastids, and discuss the main (bio)technological bottlenecks that still need to be addressed to develop robust and sustainable green cell biofactories.

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Chloroplast-localized translation for protein targeting in Chlamydomonas reinhardtii

Cited by 4 publications

References 44 publications

Chloroplast Proteostasis: Import, Sorting, Ubiquitination, and Proteolysis

Chloroplast Proteostasis: Import, Sorting, Ubiquitination, and Proteolysis

Assembly and Repair of Photosystem II in Chlamydomonas reinhardtii

Harnessing the Algal Chloroplast for Heterologous Protein Production

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