ArticleJournal of molecular biology2017
Determinants of Helix Formation for a Kv1.3 Transmembrane Segment inside the Ribosome Exit Tunnel.
Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Early-stage Determinants of T1-S1 Conformations in Kv1.3 Channels.Journal of molecular biology · 2025Article
- Disease-associated Kv1.3 Variants are Energy Compromised with Impaired Nascent Chain Folding.Journal of molecular biology · 2025Article
- The cellular pathways that maintain the quality control and transport of diverse potassium channels.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Article
- An epilepsy-associated KProceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Code Within a Code: How Codons Fine-Tune Protein Folding in the Cell.Biochemistry. Biokhimiia · 2021Review
- Transmembrane but not soluble helices fold inside the ribosome tunnel.Nature communications · 2018Article
- Investigating the Effect of Chain Connectivity on the Folding of a Beta-Sheet Protein On and Off the Ribosome.Journal of molecular biology · 2018Article
- Modulating long-range energetics via helix stabilization: A case study using T4 lysozyme.Protein science : a publication of the Protein Society · 2018Article
- Unraveling co-translational protein folding: Concepts and methods.Methods (San Diego, Calif.) · 2018Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Proteins begin to fold in the ribosome, and misfolding has pathological consequences. Among the earliest folding events in biogenesis is the formation of a helix, an elementary structure that is ubiquitously present and required for correct protein folding in all proteomes. The determinants underlying helix formation in the confined space of the ribosome exit tunnel are relatively unknown. We chose the second transmembrane segment, S2, of a voltage-gated potassium channel, Kv1.3, as a model to probe this issue. Since the N terminus of S2 is initially in an extended conformation in the folding vestibule of the ribosome yet ultimately emerges at the exit port as a helix, S2 is ideally suited for delineating sequential events and folding determinants of helix formation inside the ribosome. We show that S2's extended N terminus inside the tunnel is converted into a helix by a single, distant mutation in the nascent peptide. This transition depends on nascent peptide sequence at specific tunnel locations. Co-translational secondary folding of nascent chains inside the ribosome has profound physiological consequences that bear on correct membrane insertion, tertiary folding, oligomerization, and biochemical modification of the newborn protein during biogenesis.
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Registered trials
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