ArticleThe Journal of biological chemistry2010
Identification of protein-protein and protein-ribosome interacting regions of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Substrate-induced assembly and functional mechanism of the membrane protein insertase SecYEG-YidC.The EMBO journal · 2026Article
- Overcoming aggregation-induced quenching in DNA-assembled rhodamine dimers.Physical chemistry chemical physics : PCCP · 2025Article
- Mutation of the PEBP-like domain of the mitoribosomal MrpL35/mL38 protein results in production of nascent chains with impaired capacity to assemble into OXPHOS complexes.Molecular biology of the cell · 2023Article
- NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes.International journal of molecular sciences · 2023Article
- Probing Oxidant Effects on Superoxide Dismutase 1 Oligomeric States in Live Cells Using Single-Molecule Fluorescence Anisotropy.Chemical & biomedical imaging · 2023Article
- Ovarian carcinoma immunoreactive antigen-like protein 2 (OCIAD2) is a novel complex III-specific assembly factor in mitochondria.Molecular biology of the cell · 2022Article
- Mitochondrial OXPHOS Biogenesis: Co-Regulation of Protein Synthesis, Import, and Assembly Pathways.International journal of molecular sciences · 2020Review
- Article
- Building the CuThe Journal of biological chemistry · 2018Review
- MrpL35, a mitospecific component of mitoribosomes, plays a key role in cytochromeMolecular biology of the cell · 2017Article
- Human mitochondrial cytochromeThe Journal of biological chemistry · 2017Article
- Dynamic Editome of Zebrafish under Aminoglycosides Treatment and Its Potential Involvement in Ototoxicity.Frontiers in pharmacology · 2017Article
- Genome evolution in the cold: Antarctic icefish muscle transcriptome reveals selective duplications increasing mitochondrial function.Genome biology and evolution · 2013Article
- Structural aspects of mitochondrial translational apparatus.Current opinion in structural biology · 2012Review
- Oxa1-ribosome complexes coordinate the assembly of cytochrome C oxidase in mitochondria.The Journal of biological chemistry · 2012Article
- Mechanisms for quality control of misfolded transmembrane proteins.Biochimica et biophysica acta · 2012Review
- Interaction of α-synuclein with vesicles that mimic mitochondrial membranes.Biochimica et biophysica acta · 2012Article
- Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle.Molecular biology of the cell · 2012Article
- Mechanism of protein biosynthesis in mammalian mitochondria.Biochimica et biophysica actaReview
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3 authors.
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Abstract
The mammalian mitochondrial inner membrane protein Oxa1L is involved in the insertion of a number of mitochondrial translation products into the inner membrane. During this process, the C-terminal tail of Oxa1L (Oxa1L-CTT) binds mitochondrial ribosomes and is believed to coordinate the synthesis and membrane insertion of the nascent chains into the membrane. The C-terminal tail of Oxa1L does not contain any Cys residues. Four variants of this protein with a specifically placed Cys residue at position 4, 39, 67, or 94 of Oxa1L-CTT have been prepared. These Cys residues have been derivatized with a fluorescent probe, tetramethylrhodamine-5-maleimide, for biophysical studies. Oxa1L-CTT forms oligomers cooperatively with a binding constant in the submicromolar range. Fluorescence anisotropy and fluorescence lifetime measurements indicate that contacts near a long helix close to position 39 of Oxa1L-CTT occur during oligomer formation. Fluorescence correlation spectroscopy measurements demonstrate that all of the Oxa1L-CTT derivatives bind to mammalian mitochondrial ribosomes. Steady-state fluorescence quenching and fluorescence lifetime data indicate that there are extensive contacts between Oxa1L-CTT and the ribosome-encompassing regions around positions 39, 67, and 94. The results of this study suggest that Oxa1L-CTT undergoes conformational changes and induced oligomer formation when it binds to the ribosome.
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