ArticleJournal of bacteriology2003
Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 60 citations in OpenAlex.
- 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
- 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
- Genomic and transcriptomic profiling of phoenix colonies.Scientific reports · 2022Article
- Co-crystalization reveals the interaction between AtYchF1 and ppGpp.Frontiers in molecular biosciences · 2022Article
- The Role of the Universally Conserved ATPase YchF/Ola1 in Translation Regulation during Cellular Stress.Microorganisms · 2021Review
- Developmentally regulated GTPases: structure, function and roles in disease.Cellular and molecular life sciences : CMLS · 2021Review
- The Universally Conserved ATPase YchF Regulates Translation of Leaderless mRNA in Response to Stress Conditions.Frontiers in molecular biosciences · 2021Article
- Review
- The Impact of the Stringent Response on TRAFAC GTPases and Prokaryotic Ribosome Assembly.Cells · 2019Review
- Genomic and Proteomic Analyses ofFrontiers in microbiology · 2018Article
- The Genomic Potentials of NOB and ComammoxFrontiers in microbiology · 2018Article
- OLA1, a Translational Regulator of p21, Maintains Optimal Cell Proliferation Necessary for Developmental Progression.Molecular and cellular biology · 2016Article
- 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
- OLA1 contributes to epithelial-mesenchymal transition in lung cancer by modulating the GSK3β/snail/E-cadherin signaling.Oncotarget · 2016Article
- Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1.Antioxidants & redox signaling · 2016Article
- Article
- OLA1 regulates protein synthesis and integrated stress response by inhibiting eIF2 ternary complex formation.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The bacterial protein encoded by the gene ychF is 1 of 11 universally conserved GTPases and the only one whose function is unknown. The crystal structure determination of YchF was sought to help with the functional assignment of the protein. The YchF protein from Haemophilus influenzae was cloned and expressed, and the crystal structure was determined at 2.4 A resolution. The polypeptide chain is folded into three domains. The N-terminal domain has a mononucleotide binding fold typical for the P-loop NTPases. An 80-residue domain next to it has a pronounced alpha-helical coiled coil. The C-terminal domain features a six-stranded half-barrel that curves around an alpha-helix. The crablike three-domain structure of YchF suggests the binding site for a double-stranded nucleic acid in the cleft between the domains. The structure of the putative GTP-binding site is consistent with the postulated guanine specificity of the protein. Fluorescence measurements have demonstrated the ability of YchF to bind a double-stranded nucleic acid and GTP. Taken together with other experimental data and genomic analysis, these results suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translation factor.
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Registered trials
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.