ArticleProceedings of the National Academy of Sciences of the United States of America2005
Effect of protein structure on mitochondrial import.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Elevated mitochondrial protein import in acute myeloid leukemia increases reliance on mitochondrial protease LONP1.The Journal of clinical investigation · 2026Article
- Mitochondrial presequences harbor variable strengths to maintain organellar function.The Journal of cell biology · 2026Article
- The local mechanostructural properties of protein cargoes regulate nucleocytoplasmic transport.Nature physics · 2026Article
- Structural anisotropy results in mechano-directional transport of proteins across nuclear pores.Nature physics · 2024Article
- High-throughput colocalization pipeline quantifies efficacy of mitochondrial targeting signals across different protein types.bioRxiv : the preprint server for biology · 2023Article
- Phosphorylation of Thr9 Affects the Folding Landscape of the N-Terminal Segment of Human AGT Enhancing Protein Aggregation of Disease-Causing Mutants.Molecules (Basel, Switzerland) · 2022Article
- Compact zinc finger base editors that edit mitochondrial or nuclear DNA in vitro and in vivo.Nature communications · 2022Article
- The SecA motor generates mechanical force during protein translocation.Nature communications · 2020Article
- Free-energy landscapes of membrane co-translocational protein unfolding.Communications biology · 2020Article
- Synonymous codon substitutions perturb cotranslational protein folding in vivo and impair cell fitness.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A Synthetic Biology Workflow Reveals Variation in Processing and Solubility of Nitrogenase Proteins Targeted to Plant Mitochondria, and Differing Tolerance of Targeting Sequences in a Bacterial Nitrogenase Assay.Frontiers in plant science · 2020Article
- Detection of Internal Matrix Targeting Signal-like Sequences (iMTS-Ls) in Mitochondrial Precursor Proteins Using the TargetP Prediction Tool.Bio-protocol · 2018Article
- Periodic forces trigger knot untying during translocation of knotted proteins.Scientific reports · 2016Article
- Mutations of human NARS2, encoding the mitochondrial asparaginyl-tRNA synthetase, cause nonsyndromic deafness and Leigh syndrome.PLoS genetics · 2015Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Quantifying the role of chaperones in protein translocation by computational modeling.Frontiers in molecular biosciences · 2015Article
- Protein unfolding by biological unfoldases: insights from modeling.Biophysical journal · 2014Article
- Protein homeostasis defects of alanine-glyoxylate aminotransferase: new therapeutic strategies in primary hyperoxaluria type I.BioMed research international · 2013Review
- Evidence of evolutionary constraints that influences the sequence composition and diversity of mitochondrial matrix targeting signals.PloS one · 2013Article
- Similarities between protein folding and granular jamming.Nature communications · 2012Article
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Authors and funding
4 authors.
Funding
Abstract
Most proteins that are to be imported into the mitochondrial matrix are synthesized as precursors, each composed of an N-terminal targeting sequence followed by a mature domain. Precursors are recognized through their targeting sequences by receptors at the mitochondrial surface and are then threaded through import channels into the matrix. Both the targeting sequence and the mature domain contribute to the efficiency with which proteins are imported into mitochondria. Precursors must be in an unfolded conformation during translocation. Mitochondria can unfold some proteins by changing their unfolding pathways. The effectiveness of this unfolding mechanism depends on the local structure of the mature domain adjacent to the targeting sequence. This local structure determines the extent to which the unfolding pathway can be changed and, therefore, the unfolding rate increased. Atomic force microscopy studies find that the local structures of proteins near their N and C termini also influence their resistance to mechanical unfolding. Thus, protein unfolding during import resembles mechanical unfolding, and the specificity of import is determined by the resistance of the mature domain to unfolding as well as by the properties of the targeting sequence.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.