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Showing 1–14 of 14 results
Advanced filters: Author: Shu-ou Shan Clear advanced filters
  • Conjugation of ubiquitin chains onto proteins is an important post-translational modification that regulates the stability, localization and activity of substrate proteins. A series of enzymes known as E1, E2 and E3 mediate assembly of ubiquitin chains but the pathway remains unclear. Theoretical and experimental methodologies are now introduced to study the formation of ubiquitin chains at millisecond time resolution, demonstrating that substrate polyubiquitylation proceeds sequentially.

    • Nathan W. Pierce
    • Gary Kleiger
    • Raymond J. Deshaies
    Research
    Nature
    Volume: 462, P: 615-619
  • Newly synthesized tail-anchored membrane proteins (TAs) are relayed in a chaperone triad, Hsp70, Sgt2, and Get3, for delivery to the endoplasmic reticulum. Here, the authors show how the conformational dynamics of the cochaperone Sgt2 generates a decision point to enable efficient and selective TA targeting.

    • Hyunju Cho
    • Yumeng Liu
    • Shu-ou Shan
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16
  • Nascent peptides with signal sequences must be recognized in order to be correctly targeted within the cell. The cryo-EM structure of the E. coli signal recognition particle in complex with its receptor and the translating ribosome is now presented, indicating conformational changes that lead to receptor recruitment.

    • Leandro F Estrozi
    • Daniel Boehringer
    • Christiane Schaffitzel
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 88-90
  • Using a combination of ribosome profiling methods, Zhu et al. investigate the principles governing the cotranslational interaction of SecA with nascent proteins and reveal a hierarchical organization of protein export pathways in bacteria.

    • Zikun Zhu
    • Shuai Wang
    • Shu-ou Shan
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-15
  • Biochemistry combined with biophysical measurements and mathematical modeling offer insight into the mechanism by which the cotranslational chaperone, nascent polypeptide-associated complex (NAC), modulates substrate selection by signal recognition particle (SRP) and reduces aberrant, nonspecific targeting of ribosomes to the ER.

    • Hao-Hsuan Hsieh
    • Jae Ho Lee
    • Shu-ou Shan
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-20
  • Membrane proteins require chaperones to keep them soluble and translocation-competent. New studies have identified a chloroplast signal recognition particle, cpSRP43, as a highly specific, ATP-independent chaperone that efficiently reverses aggregation of its substrate proteins by specific binding interactions between the chaperone and its substrate.

    • Peera Jaru-Ampornpan
    • Kuang Shen
    • Shu-ou Shan
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 696-702
  • Membrane proteins are inserted co-transnationally through the association between ribosome, the signal recognition particle and its receptor, and the membrane-bound translocon. Here the authors present a cryo-EM reconstruction of this quaternary complex in the activated state and propose a model for signal sequence transfer to the translocon.

    • Ahmad Jomaa
    • Yu-Hsien Hwang Fu
    • Nenad Ban
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-9
  • The signal recognition particle (SRP) targets nascent proteins with hydrophobic signal sequences to translocation machineries at the target membrane. Structural, thermodynamic and kinetic studies of a 'false' early complex, formed by SRP and its receptor with ribosomes translating an incorrect cargo, suggest an unstable complex that rearranges inefficiently into subsequent conformational states, resulting in receptor dissociation rather than successful targeting.

    • Ottilie von Loeffelholz
    • Kèvin Knoops
    • Christiane Schaffitzel
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 604-610
  • Tail-anchor proteins are targeted post-translationally to the endoplasmic reticulum via the conserved GET pathway, in which the Get4–Get5 complex mediates delivery of substrates to Get3, the central targeting factor. The crystal structure of the ATP-bound Get3–Get4–Get5 complex and functional analyses reveal how Get4–Get5 primes Get3 for substrate loading.

    • Harry B Gristick
    • Meera Rao
    • William M Clemons Jr
    Research
    Nature Structural & Molecular Biology
    Volume: 21, P: 437-442
  • Single-molecule fluorescence microscopy techniques are used to elucidate features of the highly conserved protein-targeting machinery known as the signal recognition particle (SRP); the long SRP RNA is shown to be crucial for correct timing and precision of cargo handover to the protein-translocation machinery, a finding that could help to explain how other ribonucleosome complexes function during complex cellular processes.

    • Kuang Shen
    • Sinan Arslan
    • Shu-ou Shan
    Research
    Nature
    Volume: 492, P: 271-275