ArticleBiochemistry2017
Native Mass Spectrometry Analysis of Oligomerization States of Fluorescence Recovery Protein and Orange Carotenoid Protein: Two Proteins Involved in the Cyanobacterial Photoprotection Cycle.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- Native Mass Spectrometry Reveals Binding Modes of the Tumor Suppressor Protein p53 to Different DNA Response Elements.Journal of the American Society for Mass Spectrometry · 2026Article
- Mass spectrometry reveals the evolutionary conservation of phycobiliprotein complexes.Nature communications · 2026Article
- Article
- The increasing role of structural proteomics in cyanobacteria.Essays in biochemistry · 2023Review
- Review
- Hydrodynamic conditions affect the proteomic profile of marine biofilms formed by filamentous cyanobacterium.NPJ biofilms and microbiomes · 2022Article
- Oligomerization processes limit photoactivation and recovery of the orange carotenoid protein.Biophysical journal · 2022Article
- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
- High intracellular stability of the spidroin N-terminal domain in spite of abundant amyloidogenic segments revealed by in-cell hydrogen/deuterium exchange mass spectrometry.The FEBS journal · 2020Article
- Fluorescence recovery protein: a powerful yet underexplored regulator of photoprotection in cyanobacteria†.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2020Review
- Interdomain interactions reveal the molecular evolution of the orange carotenoid protein.Nature plants · 2019Article
- OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria.Nature communications · 2018Article
- Site, trigger, quenching mechanism and recovery of non-photochemical quenching in cyanobacteria: recent updates.Photosynthesis research · 2018Review
- Paralogs of the C-Terminal Domain of the Cyanobacterial Orange Carotenoid Protein Are Carotenoid Donors to Helical Carotenoid Proteins.Plant physiology · 2017Article
- The Unique Protein-to-Protein Carotenoid Transfer Mechanism.Biophysical journal · 2017Article
- A Molecular Mechanism for Nonphotochemical Quenching in Cyanobacteria.Biochemistry · 2017Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
The orange carotenoid protein (OCP) and fluorescence recovery protein (FRP) are present in many cyanobacteria and regulate an essential photoprotection cycle in an antagonistic manner as a function of light intensity. We characterized the oligomerization states of OCP and FRP by using native mass spectrometry, a technique that has the capability of studying native proteins under a wide range of protein concentrations and molecular masses. We found that dimeric FRP is the predominant state at protein concentrations ranging from 3 to 180 μM and that higher-order oligomers gradually form at protein concentrations above this range. The OCP, however, demonstrates significantly different oligomerization behavior. Monomeric OCP (mOCP) dominates at low protein concentrations, with an observable population of dimeric OCP (dOCP). The ratio of dOCP to mOCP, however, increases proportionally with protein concentration. Higher-order OCP oligomers form at protein concentrations beyond 10 μM. Additionally, native mass spectrometry coupled with ion mobility allowed us to measure protein collisional cross sections and interrogate the unfolding of different FRP and OCP oligomers. We found that monomeric FRP exhibits a one-stage unfolding process, which could be correlated with its C-terminal bent crystal structure. The structural domain compositions of FRP and OCP are compared and discussed.
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