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Showing 1–12 of 12 results
Advanced filters: Author: Tomohide Saio Clear advanced filters

  • Nuclear import receptors (NIRs) regulate self-association of RNA-binding proteins as phase modifiers, while C9orf72-derived arginine-rich polydipeptides lead to aberrant phase transitions. Here the authors show in molecular basis how arginine-rich poly-dipeptides impede the ability of NIRs, particularly Kapβ2.

    • Hitoki Nanaura
    • Honoka Kawamukai
    • Eiichiro Mori
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • Self-association of low-complexity protein sequences (LC domains) is important for polymer formation, but the mechanisms underlying cell recognition of LC domain polymers remain unclear. Here, authors show that zinc finger domains bind LC domains in a cross-β polymer-dependent manner.

    • Naohiko Iguchi
    • Noriyoshi Isozumi
    • Eiichiro Mori
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-12

  • Lee et al. show that Ca²⁺ triggers condensates enriched with PDIA6, an ER-resident disulfide isomerase and chaperone, along with other protein disulfide isomerase family proteins and some chaperones that in turn enhance folding of proinsulin.

    • Young-Ho Lee
    • Tomohide Saio
    • Masaki Okumura
    ResearchOpen Access
    Nature Cell Biology
    Volume: 27, P: 1952-1964

  • The mechanism underlying the formation of ionophore polyethers—polyketide-derived natural products containing tetrahydrofuran and tetrahydropyran rings—has been elusive. Now structural and biochemical analyses reveal that a C26 linear precursor undergoes four successive cyclizations within the single active site of the heterodimeric polyether epoxide hydrolase MonBI·MonBII, in which MonBI promotes MonBII’s folded active conformation.

    • Nana Yabuno
    • Atsushi Minami
    • Toyoyuki Ose
    Research
    Nature Chemistry
    P: 1-10

  • The three-dimensional structure of a key complex in chaperone-mediated protein disaggregation, comprising ClpB and DnaK, has been determined using NMR. In addition to providing unique mechanistic insights, the approach promises to elucidate the structural basis for the assembly of elusive dynamic protein machineries in the near future.

    • Tomohide Saio
    • Charalampos G Kalodimos
    News & Views
    Nature Structural & Molecular Biology
    Volume: 20, P: 409-410

  • The regulation of meiotic prophase progression varies between males and females. This study reveals the involvement of an atypical heat shock transcription factor HSF5 in gene expression during male meiotic prophase and highlights the involved gene regulatory mechanism.

    • Saori Yoshimura
    • Ryuki Shimada
    • Kei-ichiro Ishiguro
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-22

  • ClpXP is the main ATP-dependent proteolytic complex in bacteria, is essential for maintaining cellular protein homeostasis and is also critical for bacterial pathogenesis. Here, the authors establish a functional link between ClpXP and trigger actor, a chaperone involved in the early stages of protein folding.

    • Kamran Rizzolo
    • Angela Yeou Hsiung Yu
    • Walid A. Houry
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-18

  • Single-molecule analysis by high-speed atomic force microscopy reveals that oxidized protein disulfide isomerase adopts a dynamic conformation in the absence of substrates and forms face-to-face dimers to accelerate oxidative folding in the presence of substrates.

    • Masaki Okumura
    • Kentaro Noi
    • Kenji Inaba
    Research
    Nature Chemical Biology
    Volume: 15, P: 499-509

  • The solution structure of SecB, a molecular chaperone that exhibits strong antifolding activity, in complex with alkaline phosphatase and maltose-binding protein captured in their unfolded states.

    • Chengdong Huang
    • Paolo Rossi
    • Charalampos G. Kalodimos
    Research
    Nature
    Volume: 537, P: 202-206