ArticleJournal of the American Chemical Society2013
Molecular crowding enhanced ATPase activity of the RNA helicase eIF4A correlates with compaction of its quaternary structure and association with eIF4G.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Using Solution NMR to Study the RNA-Binding Properties and Molecular Mechanisms of the RNA Helicase DDX3X.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Allosteric regulation of enzymatic catalysis by molecular crowding.Communications chemistry · 2026Article
- Molecular crowding effects on protein stability in a bacterial proteome.Scientific reports · 2026Article
- Simulating Crowding In Vitro: Not an Elusive Goal Any Longer.Sub-cellular biochemistry · 2025Review
- Varying molecular interactions explain aspects of crowder-dependent enzyme function of a viral protease.PLoS computational biology · 2023Article
- Macromolecular crowding effects on the kinetics of opposing reactions catalyzed by alcohol dehydrogenase.Biochemistry and biophysics reports · 2021Article
- A Phosphorylated Intermediate in the Activation of WNK Kinases.Biochemistry · 2020Article
- Confinement and Crowding Effects on Folding of a Multidomain Y-Family DNA Polymerase.Journal of chemical theory and computation · 2020Article
- Structural Analyses of Intrinsically Disordered Proteins by Small-Angle X-Ray Scattering.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The TYRP1-mediated protection of human tyrosinase activity does not involve stable interactions of tyrosinase domains.Pigment cell & melanoma research · 2019Article
- Effect of Macromolecular Crowding on the FMN-Heme Intraprotein Electron Transfer in Inducible NO Synthase.Biochemistry · 2019Article
- Identification of novel leishmanicidal molecules by virtual and biochemical screenings targeting Leishmania eukaryotic translation initiation factor 4A.PLoS neglected tropical diseases · 2018Article
- Large cosolutes, small cosolutes, and dihydrofolate reductase activity.Protein science : a publication of the Protein Society · 2017Article
- Emerging applications of small angle solution scattering in structural biology.Protein science : a publication of the Protein Society · 2015Review
- Beyond the excluded volume effects: mechanistic complexity of the crowded milieu.Molecules (Basel, Switzerland) · 2015Review
- What macromolecular crowding can do to a protein.International journal of molecular sciences · 2014Review
- Human translation initiation factor eIF4G1 possesses a low-affinity ATP binding site facing the ATP-binding cleft of eIF4A in the eIF4G/eIF4A complex.Biochemistry · 2014Article
- Macromolecular crowding effects on two homologs of ribosomal protein s16: protein-dependent structural changes and local interactions.Biophysical journal · 2014Article
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4 authors.
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Abstract
Enzymatic reactions occur in a crowded and confined environment in vivo, containing proteins, RNA and DNA. Previous reports have shown that interactions between macromolecules, and reactions rates differ significantly between crowded environments and dilute buffers. However, the direct effect of crowding on the level of high-resolution structures of macromolecules has not been extensively analyzed and is not well understood. Here we analyze the effect of macromolecular crowding on structure and function of the human translation initiation factors eIF4A, a two-domain DEAD-Box helicase, the HEAT-1 domain of eIF4G, and their complex. We find that crowding enhances the ATPase activity of eIF4A, which correlates with a shift to a more compact structure as revealed with small-angle X-ray scattering. However, the individual domains of eIF4A, or the eIF4G-HEAT-1 domain alone show little structural changes due to crowding except for flexible regions. Thus, the effect of macromolecular crowding on activity and structure need to be taken into account when evaluating enzyme activities and structures of multidomain proteins, proteins with flexible regions, or protein complexes obtained by X-ray crystallography, NMR, or other structural methods.
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