ArticleRNA biology2012
The 70S ribosome modulates the ATPase activity of Escherichia coli YchF.
Article in RNA biology, 2012. 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.
- The unconventional G protein AtYchF1 interacts with ribosomal protein AtRPS7 to modulate selective translation for balancing plant growth and stress responses in Arabidopsis.Plant communications · 2026Article
- From biophysical interaction to structural modeling: bi-terminal G and TGS domains drive rice OsYchF1-OsGAP1 complex formation.Botanical studies · 2025Article
- Conserved GTPase OLA1 promotes efficient translation on D/E-rich mRNA.Nature communications · 2025Article
- Article
- The Universally Conserved Unconventional G Protein YchF Is Critical for Growth and Stress Response.Life (Basel, Switzerland) · 2023Review
- Structural comparison of unconventional G protein YchF with heterotrimeric G protein and small G protein.Plant signaling & behavior · 2022Review
- The Role of the Universally Conserved ATPase YchF/Ola1 in Translation Regulation during Cellular Stress.Microorganisms · 2021Review
- High Throughput Proteomic Exploration of Hypothermic Preservation Reveals Active Processes within the Cell Associated with Cold Ischemia Kinetic.International journal of molecular sciences · 2021Article
- The Universally Conserved ATPase YchF Regulates Translation of Leaderless mRNA in Response to Stress Conditions.Frontiers in molecular biosciences · 2021Article
- Functional Analysis of BipA in E. coli Reveals the Natural Plasticity of 50S Subunit Assembly.Journal of molecular biology · 2020Article
- Capturing Membrane Protein Ribosome Nascent Chain Complexes in a Native-like Environment for Co-translational Studies.Biochemistry · 2020Article
- Article
- Construction and Use of TransposonFrontiers in microbiology · 2019Article
- ATP binding by the P-loop NTPase OsYchF1 (an unconventional G protein) contributes to biotic but not abiotic stress responses.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1.Antioxidants & redox signaling · 2016Article
- OLA1 regulates protein synthesis and integrated stress response by inhibiting eIF2 ternary complex formation.Scientific reports · 2015Article
- Histidine 114 Is Critical for ATP Hydrolysis by the Universally Conserved ATPase YchF.The Journal of biological chemistry · 2015Article
- Structural basis for the interaction of protein S1 with the Escherichia coli ribosome.Nucleic acids research · 2015Article
- Regulation of cell-matrix adhesion by OLA1, the Obg-like ATPase 1.Biochemical and biophysical research communications · 2014Article
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Authors and funding
6 authors.
Funding
Abstract
YchF is one of two universally conserved GTPases with unknown cellular function. As a first step toward elucidating YchF's cellular role, we performed a detailed biochemical characterization of the protein from Escherichia coli. Our data from fluorescence titrations not only confirmed the surprising finding that YchFE.coli binds adenine nucleotides more efficiently than guanine nucleotides, but also provides the first evidence suggesting that YchF assumes two distinct conformational states (ATP- and ADP-bound) consistent with the functional cycle of a typical GTPase. Based on an in vivo pull-down experiment using a His-tagged variant of YchF from E. coli (YchFE.coli), we were able to isolate a megadalton complex containing the 70S ribosome. Based on this finding, we report the successful reconstitution of a YchF•70S complex in vitro, revealing an affinity (KD) of the YchFE.coli•ADPNP complex for 70S ribosomes of 3 μM. The in vitro reconstitution data also suggests that the identity of the nucleotide-bound state of YchF (ADP or ATP) modulates its affinity for 70S ribosomes. A detailed Michaelis-Menten analysis of YchF's catalytic activity in the presence and the absence of the 70S ribosome and its subunits revealed for the first time that the 70S ribosome is able to stimulate YchF's ATPase activity (~10-fold), confirming the ribosome as part of the functional cycle of YchF. Our findings taken together with previously reported data for the human homolog of YchF (hOLA1) indicate a high level of evolutionary conservation in the enzymatic properties of YchF and suggest that the ribosome is the main functional partner of YchF not only in bacteria.
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