scholarly journals Role of ClpP in the Biogenesis and Degradation of RuBisCO and ATP Synthase in Chlamydomonas reinhardtii

Plants ◽  
2019 ◽  
Vol 8 (7) ◽  
pp. 191 ◽  
Author(s):  
Majeran ◽  
Wostrikoff ◽  
Wollman ◽  
Vallon
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Atp Synthase ◽  
Co2 Fixation ◽  
Inorganic Carbon ◽  
Point Mutations ◽  
Clp Protease ◽  
Bisphosphate Carboxylase ◽  
N Starvation ◽  
Sulfur Containing

Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) associates a chloroplast- and a nucleus-encoded subunit (LSU and SSU). It constitutes the major entry point of inorganic carbon into the biosphere as it catalyzes photosynthetic CO2 fixation. Its abundance and richness in sulfur-containing amino acids make it a prime source of N and S during nutrient starvation, when photosynthesis is downregulated and a high RuBisCO level is no longer needed. Here we show that translational attenuation of ClpP1 in the green alga Chlamydomonas reinhardtii results in retarded degradation of RuBisCO during S- and N-starvation, suggesting that the Clp protease is a major effector of RubisCO degradation in these conditions. Furthermore, we show that ClpP cannot be attenuated in the context of rbcL point mutations that prevent LSU folding. The mutant LSU remains in interaction with the chloroplast chaperonin complex. We propose that degradation of the mutant LSU by the Clp protease is necessary to prevent poisoning of the chaperonin. In the total absence of LSU, attenuation of ClpP leads to a dramatic stabilization of unassembled SSU, indicating that Clp is responsible for its degradation. In contrast, attenuation of ClpP in the absence of SSU does not lead to overaccumulation of LSU, whose translation is controlled by assembly. Altogether, these results point to RuBisCO degradation as one of the major house-keeping functions of the essential Clp protease. In addition, we show that non-assembled subunits of the ATP synthase are also stabilized when ClpP is attenuated. In the case of the atpA-FUD16 mutation, this can even allow the assembly of a small amount of CF1, which partially restores phototrophy.

The role of the chloroplast in inorganic carbon acquisition by Chlamydomonas reinhardtii

1991 ◽  
Vol 69 (5) ◽  
pp. 1017-1024 ◽  
Author(s):  
James V. Moroney ◽  
Catherine B. Mason
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Inorganic Carbon ◽  
Published Data ◽  
Carbon Uptake ◽  
Intact Chloroplasts ◽  
Inorganic Carbon Transport ◽  
Inorganic Carbon Uptake ◽  
Carbon Transport ◽  
Inorganic Carbon Acquisition

The role of the chloroplast in algal inorganic carbon acquisition is reviewed. Unicellular green algae possess the ability to grow photoautotrophically at very low CO2 concentrations. The presence of a CO2-concentrating system that elevates the CO2 level within the cell can account for the algae's ability to reduce photorespiration and grow under these conditions. The mechanism of this inorganic carbon transport is unclear at present, although both the plasmalemma and the chloroplast have been implicated in this process. Three aspects of the role of the chloroplast in Chlamydomonas reinhardtii inorganic carbon uptake are discussed in this review. First, the present models of inorganic carbon uptake are summarized. Second, the purity and integrity of intact chloroplast preparations are discussed. Third, an evaluation of the published data on inorganic carbon uptake by isolated intact chloroplasts is presented. Key words: Chlamydomonas reinhardtii, carbonic anhydrase, chloroplast, active CO2 uptake.

scholarly journals Effects of mutations at the two processing sites of the precursor for the small subunit of ribulose-bisphosphate carboxylase in Chlamydomonas reinhardtii

2002 ◽  
Vol 366 (3) ◽  
pp. 989-998 ◽  
Author(s):  
Cédric INVERNIZZI ◽  
Jonathan IMHOF ◽  
Gabriela BURKARD ◽  
Katharina SCHMID ◽  
Arminio BOSCHETTI
Keyword(s):  
Amino Acids ◽  
Chlamydomonas Reinhardtii ◽  
Small Subunit ◽  
Ribulose Bisphosphate Carboxylase ◽  
Cleavage Sites ◽  
Bisphosphate Carboxylase ◽  
Molecular Masses ◽  
Processing Site

The role of the two processing sites in the precursor of the small subunit (SS) of ribulose-1,5-bisphosphate carboxylase/oxygenase (pSS) of Chlamydomonas reinhardtii was studied by introducing mutations at the cleavage sites for the stromal processing peptidases SPP-1 and SPP-2, which hydrolyse wild-type pSS (20.6kDa) to an intermediate-sized product iSS (18.3kDa) and to the mature SS (16.3kDa), respectively. The mutations introduced into cDNA resulted in exchange of (a) two amino acids flanking processing site 1, or (b) one or (c) both amino acids flanking processing site 2. Mutation (a) prevented pSS from being processed at site 1 but not from cleavage at site 2. Mutation (c) abolished the action of SPP-2 but not SPP-1. When pSS with mutation (c) was imported into isolated chloroplasts, iSS accumulated while SS formation was abolished. However, mature SS was produced even in the absence of iSS synthesis (mutation a). Import of pSS bearing mutation (b), which only partially inhibited processing at the SPP-2 site, slowed the rate of SS formation down whereas iSS and some slightly smaller derivatives accumulated. These experiments suggested that in Chlamydomonas processing of pSS can occur in two steps, whereby the first step is facultative. The same three mutations were studied in vivo after transformation of SS-deficient C. reinhardtii T60-3 with mutated genomic DNA. Growth and photosynthesis was as in control transformants, except for the slower-growing transformants (mutation c) where no mature SS was immuno-detected. However, pSS fragments with molecular masses between those of iSS and SS were present even in the ribulose-1,5-bisphosphate carboxylase/oxygenase holoenzyme.

The role of the chloroplast in inorganic carbon uptake by eukaryotic algae

1998 ◽  
Vol 76 (6) ◽  
pp. 1025-1034 ◽  
Author(s):  
James V Moroney ◽  
Zhi-Yuan Chen
Keyword(s):  
Carbonic Anhydrase ◽  
Alternative Explanation ◽  
Inorganic Carbon ◽  
Large Majority ◽  
Carbon Uptake ◽  
Bisphosphate Carboxylase ◽  
Eukaryotic Algae ◽  
Growth Regime ◽  
Inorganic Carbon Uptake

The role of the chloroplast in the adaptation to low CO2 by eukaryotic algae is reviewed. Eukaryotic algae can grow on very low CO2 levels because of the presence of a CO2 concentrating mechanism (CCM). This review is focused on the localization of key photosynthetic enzymes such as ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) and carbonic anhydrase as well as the location of presumptive components of the CCM and photorespiratory cycle within the chloroplast. Previous immunolocalization studies place as much as 99% or as little as 5% of the cell's Rubisco in the chloroplast pyrenoid. These different results are summarized, and an alternative explanation is provided. The different results appear to be due to the growth regime of the algae as well as differences in quantitation. Evidence suggests that a large majority of Rubisco is located within the pyrenoid. We have also summarized the recent discovery of a thylakoid-bound carbonic anhydrase that is essential to growth on low CO2. A model depicting a possible role for this carbonic anhydrase in photosynthesis is presented.Key words: chloroplast, algae, pyrenoid, carbonic anhydrase, photosynthesis.

scholarly journals A Theoretical Model of Mitochondrial ATP Synthase Deficiencies. The Role of Mitochondrial Carriers

Processes ◽  
2021 ◽  
Vol 9 (8) ◽  
pp. 1424
Author(s):  
Jean-Pierre Mazat ◽  
Anne Devin ◽  
Edgar Yoboue ◽  
Stéphane Ransac
Keyword(s):  
Atp Synthase ◽  
Point Mutations ◽  
Atp Synthesis ◽  
Yeast Saccharomyces Cerevisiae ◽  
Complex Iv ◽  
Equivalent Point ◽  
Mitochondrial Atp Synthase ◽  
Atp6 Gene ◽  
Substrate Level

The m.8993T>G mutation of the mitochondrial MT-ATP6 gene is associated with NARP syndrome (neuropathy, ataxia and retinitis pigmentosa). The equivalent point mutation introduced in yeast Saccharomyces cerevisiae mitochondrial DNA considerably reduced the activity of ATP synthase and of cytochrome-c-oxidase, preventing yeast growth on oxidative substrates. The overexpression of the mitochondrial oxodicarboxylate carrier (Odc1p) was able to rescue the growth on the oxidative substrate by increasing the substrate-level phosphorylation of ADP coupled to the conversion of α-ketoglutarate (AKG) into succinate with an increase in Complex IV activity. Previous studies showed that equivalent point mutations in ATP synthase behave similarly and can be rescued by Odc1p overexpression and/or the uncoupling of OXPHOS from ATP synthesis. In order to better understand the mechanism of the ATP synthase mutation bypass, we developed a core model of mitochondrial metabolism based on AKG as a respiratory substrate. We describe the different possible metabolite outputs and the ATP/O ratio values as a function of ATP synthase inhibition.

Role of key point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein

2020 ◽  
Vol 20 ◽  
Author(s):  
Bipin Singh
Keyword(s):  
Receptor Binding ◽  
Point Mutations ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Spike Glycoprotein ◽  
Angiotensin Converting Enzyme 2 ◽  
Recent Outbreak ◽  
Novel Coronavirus ◽  
Genomic Similarity

: The recent outbreak of novel coronavirus (SARS-CoV-2 or 2019-nCoV) and its worldwide spread is posing one of the major threats to human health and the world economy. It has been suggested that SARS-CoV-2 is similar to SARSCoV based on the comparison of the genome sequence. Despite the genomic similarity between SARS-CoV-2 and SARSCoV, the spike glycoprotein and receptor binding domain in SARS-CoV-2 shows the considerable difference compared to SARS-CoV, due to the presence of several point mutations. The analysis of receptor binding domain (RBD) from recently published 3D structures of spike glycoprotein of SARS-CoV-2 (Yan, R., et al. (2020); Wrapp, D., et al. (2020); Walls, A. C., et al. (2020)) highlights the contribution of a few key point mutations in RBD of spike glycoprotein and molecular basis of its efficient binding with human angiotensin-converting enzyme 2 (ACE2).

scholarly journals Four Mutant Alleles Elucidate the Role of the G2 Protein in the Development of C4 and C3 Photosynthesizing Maize Tissues

Genetics ◽  
2001 ◽  
Vol 159 (2) ◽  
pp. 787-797
Author(s):  
Lizzie Cribb ◽  
Lisa N Hall ◽  
Jane A Langdale
Keyword(s):  
Cell Types ◽  
Bundle Sheath ◽  
Primary Role ◽  
Ribulose Bisphosphate Carboxylase ◽  
Sheath Cell ◽  
Mesophyll Cells ◽  
Phenotypic Data ◽  
Bisphosphate Carboxylase ◽  
Bundle Sheath Cell

Abstract Maize leaf blades differentiate dimorphic photosynthetic cell types, the bundle sheath and mesophyll, between which the reactions of C4 photosynthesis are partitioned. Leaf-like organs of maize such as husk leaves, however, develop a C3 pattern of differentiation whereby ribulose bisphosphate carboxylase (RuBPCase) accumulates in all photosynthetic cell types. The Golden2 (G2) gene has previously been shown to play a role in bundle sheath cell differentiation in C4 leaf blades and to play a less well-defined role in C3 maize tissues. To further analyze G2 gene function in maize, four g2 mutations have been characterized. Three of these mutations were induced by the transposable element Spm. In g2-bsd1-m1 and g2-bsd1-s1, the element is inserted in the second intron and in g2-pg14 the element is inserted in the promoter. In the fourth case, g2-R, four amino acid changes and premature polyadenylation of the G2 transcript are observed. The phenotypes conditioned by these four mutations demonstrate that the primary role of G2 in C4 leaf blades is to promote bundle sheath cell chloroplast development. C4 photosynthetic enzymes can accumulate in both bundle sheath and mesophyll cells in the absence of G2. In C3 tissue, however, G2 influences both chloroplast differentiation and photosynthetic enzyme accumulation patterns. On the basis of the phenotypic data obtained, a model that postulates how G2 acts to facilitate C4 and C3 patterns of tissue development is proposed.

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