ArticleProceedings of the National Academy of Sciences of the United States of America2014
Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. 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, 32 citations in OpenAlex.
- The NSvc4 Protein of Rice Stripe Virus Suppresses Chloroplast-Mediated Defense by Interacting with NbPsbQ.International journal of molecular sciences · 2026Article
- Review
- MEMBRANE PROTEIN STRUCTURES AND INTERACTIONS FROM COVALENT LABELING COUPLED WITH MASS SPECTROMETRY.Mass spectrometry reviews · 2022Review
- The spatial network of skeletal proteins in a stony coral.Journal of the Royal Society, Interface · 2021Article
- Reciprocal Effect of Copper and Iron Regulation on the Proteome ofFrontiers in bioengineering and biotechnology · 2021Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- The catalytic mechanism of electron-bifurcating electron transfer flavoproteins (ETFs) involves an intermediary complex with NAD<sup/>.The Journal of biological chemistry · 2019Article
- The Role of Mass Spectrometry in Structural Studies of Flavin-Based Electron Bifurcating Enzymes.Frontiers in microbiology · 2018Review
- In vivo system for analyzing the function of the PsbP protein using Chlamydomonas reinhardtii.Photosynthesis research · 2017Article
- Article
- The extrinsic proteins of photosystem II: update.Planta · 2016Review
- Novel Features of Eukaryotic Photosystem II Revealed by Its Crystal Structure Analysis from a Red Alga.The Journal of biological chemistry · 2016Article
- Dramatic Domain Rearrangements of the Cyanobacterial Orange Carotenoid Protein upon Photoactivation.Biochemistry · 2016Article
- The N-terminal sequence of the extrinsic PsbP protein modulates the redox potential of Cyt b559 in photosystem II.Scientific reports · 2016Article
- The Use of Advanced Mass Spectrometry to Dissect the Life-Cycle of Photosystem II.Frontiers in plant science · 2016Review
- Structural Coupling of Extrinsic Proteins with the Oxygen-Evolving Center in Photosystem II.Frontiers in plant science · 2016Review
- The Use of Contact Mode Atomic Force Microscopy in Aqueous Medium for Structural Analysis of Spinach Photosynthetic Complexes.Plant physiology · 2015Article
- Resonance assignment of PsbP: an extrinsic protein from photosystem II of Spinacia oleracea.Biomolecular NMR assignments · 2015Article
- Isolation of Plant Photosystem II Complexes by Fractional Solubilization.Frontiers in plant science · 2015Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Protein cross-linking and radiolytic footprinting coupled with high-resolution mass spectrometry were used to examine the structure of PsbP and PsbQ when they are bound to Photosystem II. In its bound state, the N-terminal 15-amino-acid residue domain of PsbP, which is unresolved in current crystal structures, interacts with domains in the C terminus of the protein. These interactions may serve to stabilize the structure of the N terminus and may facilitate PsbP binding and function. These interactions place strong structural constraints on the organization of PsbP when associated with the Photosystem II complex. Additionally, amino acid residues in the structurally unresolved loop 3A domain of PsbP ((90)K-(107)V), (93)Y and (96)K, are in close proximity (≤ 11.4 Å) to the N-terminal (1)E residue of PsbQ. These findings are the first, to our knowledge, to identify a putative region of interaction between these two components. Cross-linked domains within PsbQ were also identified, indicating that two PsbQ molecules can interact in higher plants in a manner similar to that observed by Liu et al. [(2014) Proc Natl Acad Sci 111(12):4638-4643] in cyanobacterial Photosystem II. This interaction is consistent with either intra-Photosystem II dimer or inter-Photosystem II dimer models in higher plants. Finally, OH(•) produced by synchrotron radiolysis of water was used to oxidatively modify surface residues on PsbP and PsbQ. Domains on the surface of both protein subunits were resistant to modification, indicating that they were shielded from water and appear to define buried regions that are in contact with other Photosystem II components.
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