ArticleBiophysical journal2012
Protein oligomerization monitored by fluorescence fluctuation spectroscopy: self-assembly of rubisco activase.
Article in Biophysical journal, 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, 51 citations in OpenAlex.
- Ribulose-1,5-bisphosphate carboxylase/oxygenase activase isoforms from diverse species show differences in oligomeric structure, thermal stability, and activity.European biophysics journal : EBJ · 2025Article
- Label-Free Anti-Brownian Trapping of Single Nanoparticles in Solution.The journal of physical chemistry. C, Nanomaterials and interfaces · 2024Article
- Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling.Frontiers in molecular biosciences · 2023Review
- Development and application of multicolor burst analysis spectroscopy.Biophysical journal · 2021Article
- Probing the rice Rubisco-Rubisco activase interaction via subunit heterooligomerization.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Resolving fluorescent species by their brightness and diffusion using correlated photon-counting histograms.PloS one · 2019Article
- Assembly-disassembly is coupled to the ATPase cycle of tobacco Rubisco activase.The Journal of biological chemistry · 2018Article
- Quantitative mass imaging of single biological macromolecules.Science (New York, N.Y.) · 2018Article
- In Vitro Characterization of Thermostable CAM Rubisco Activase Reveals a Rubisco Interacting Surface Loop.Plant physiology · 2017Article
- The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.Frontiers in molecular biosciences · 2017Review
- Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Chemical communications (Cambridge, England) · 2015Review
- Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase: product inhibition, cooperativity, and magnesium activation.The Journal of biological chemistry · 2015Article
- Application of three-photon excitation FCS to the study of protein oligomerization.The journal of physical chemistry. B · 2014Article
- Intrinsic stability and oligomerization dynamics of DNA processivity clamps.Nucleic acids research · 2014Article
- Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases.Photosynthesis research · 2014Review
- Activation of interspecies-hybrid Rubisco enzymes to assess different models for the Rubisco-Rubisco activase interaction.Photosynthesis research · 2013Article
- Small oligomers of ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase are required for biological activity.The Journal of biological chemistry · 2013Article
- Article
- An elegant way to quantitatively analyze oligomer formation in solution.Biophysical journal · 2012Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A methodology is presented to characterize complex protein assembly pathways by fluorescence correlation spectroscopy. We have derived the total autocorrelation function describing the behavior of mixtures of labeled and unlabeled protein under equilibrium conditions. Our modeling approach allows us to quantitatively consider the relevance of any proposed intermediate form, and K(d) values can be estimated even when several oligomeric species coexist. We have tested this method on the AAA+ ATPase Rubisco activase (Rca). Rca self-association regulates the CO(2) fixing activity of the enzyme Rubisco, directly affecting biomass accumulation in higher plants. However, the elucidation of its assembly pathway has remained challenging, precluding a detailed mechanistic investigation. Here, we present the first, to our knowledge, thermodynamic characterization of oligomeric states of cotton β-Rca complexed with Mg·ADP. We find that the monomer is the dominating species below 0.5 micromolar. The most plausible model supports dissociation constants of ∼4, 1, and 1 micromolar for the monomer-dimer, dimer-tetramer, and tetramer-hexamer equilibria, in line with the coexistence of four different oligomeric forms under typical assay conditions. Large aggregates become dominant above 40 micromolar, with continued assembly at even higher concentrations. We propose that under some conditions, ADP-bound Rca self-associates by forming spiral arrangements that grow along the helical axis. Other models such as the stacking of closed hexameric rings are also discussed.
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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.