ORCID Profile
0000-0002-5637-5237
Current Organisation
Australian National University
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Publisher: Elsevier BV
Date: 07-2023
Publisher: Universidade de Sao Paulo, Agencia USP de Gestao da Informacao Academica (AGUIA)
Date: 17-08-2023
DOI: 10.11606/ISSN.2316-9095.V23-208078
Abstract: This study provides new information on the deformation, metamorphism, and tectonic setting of the metavolcanic rocks of the southern portion of the Porongos Complex, southern Brazil. The structural analysis enabled the identification of three deformational phases, formed under ductile to semi-ductile conditions. D1 progressed through deformation partitioning, comprising closed to isoclinal folds and an axial plane foliation. Then, simple shear prevailed, resulting in isoclinal folds, sigma-type porphyroclasts, foliation transposition, and mylonitic rocks. D2 comprises open to gentle folds and an axial plane cleavage. The formation of shear bands is ascribed to the semi-ductile D3. The mineral assemblage represented by phengite + chlorite + clinozoisite-epidote + actinolite + albite + quartz associated with the temperatures obtained through the chlorite geothermometer (316°C) indicates greenschist facies conditions. The protoliths of these metavolcanic rocks are geochemically discriminated as calc-alkaline, dacite-to-rhyodacite, with peraluminous compositions. The bulk trace element compositions show enrichment in large-ion lithophile elements and light rare-earth elements and depletion in heavy rare-earth elements. Also, negative Nb, P, Ti, and Ta anomalies are observed in the multielement diagram. All these geochemical features are typical of rocks formed in continental magmatic arcs. Geochemical comparison with other pre-collisional Tonian orthometamorphic rocks from the Dom Feliciano Belt demonstrates strong similarities, which corroborates the prior interpretation of a continental arc setting for the origin of these Tonian rocks.
Publisher: Oxford University Press (OUP)
Date: 22-02-2021
Abstract: ATP is generated in mitochondria by oxidative phosphorylation. Complex I (NADH:ubiquinone oxidoreductase or NADH dehydrogenase) is the first multisubunit protein complex of this pathway, oxidizing NADH and transferring electrons to the ubiquinone pool. Typically, Complex I mutants display a slow growth rate compared to wild-type plants. Here, using a forward genetic screen approach for restored growth of a Complex I mutant, we have identified the mitochondrial ATP-dependent metalloprotease, Filamentous Temperature Sensitive H 3 (FTSH3), as a factor that is required for the disassembly of Complex I. An ethyl methanesulfonate-induced mutation in FTSH3, named as rmb1 (restoration of mitochondrial biogenesis 1), restored Complex I abundance and plant growth. Complementation could be achieved with FTSH3 lacking proteolytic activity, suggesting the unfoldase function of FTSH3 has a role in Complex I disassembly. The introduction of the rmb1 to an additional, independent, and extensively characterized Complex I mutant, ndufs4, resulted in similar increases to Complex I abundance and a partial restoration of growth. These results show that disassembly or degradation of Complex I plays a role in determining its steady-state abundance and thus turnover may vary under different conditions.
Publisher: Elsevier BV
Date: 09-2022
Publisher: Portland Press Ltd.
Date: 19-05-2022
DOI: 10.1042/BST20220195
Abstract: Mitochondrial function relies on the homeostasis and quality control of their proteome, including components of the oxidative phosphorylation (OXPHOS) pathway that generates energy in form of ATP. OXPHOS subunits are under constant exposure to reactive oxygen species due to their oxidation-reduction activities, which consequently make them prone to oxidative damage, misfolding, and aggregation. As a result, quality control mechanisms through turnover and degradation are required for maintaining mitochondrial activity. Degradation of OXPHOS subunits can be achieved through proteomic turnover or modular degradation. In this review, we present multiple protein degradation pathways in plant mitochondria. Specifically, we focus on the intricate turnover of OXPHOS subunits, prior to protein import via cytosolic proteasomal degradation and post import and assembly via intra-mitochondrial proteolysis involving multiple AAA+ proteases. Together, these proteolytic pathways maintain the activity and homeostasis of OXPHOS components.
No related grants have been discovered for Rodrigo Rodrigues.