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Title: Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II

Abstract

We used protein cross-linking and radiolytic footprinting coupled with high-resolution mass spectrometry to examine the structure of PsbP and PsbQ when they are bound to Photosystem II, in this paper. 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 (90K–107V), 93Y and 96K, are in close proximity (≤11.4 Å) to the N-terminal 1E residue of PsbQ. Our 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. Furthermore, this interaction is consistent with either intra-Photosystem II dimer or inter-Photosystem II dimer models in higher plants.more » Finally, OH• produced by synchrotron radiolysis of water was used to oxidatively modify surface residues on PsbP and PsbQ. Finally, 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.« less

Authors:
 [1];  [1];  [2];  [3];  [2];  [4];  [3];  [1]
  1. Louisiana State Univ., Baton Rouge, LA (United States). Dept. of Biological Sciences
  2. Louisiana State Univ., Baton Rouge, LA (United States). J. Bennett Johnston Sr. Center for Advanced Microstructures and Devices
  3. Univ. of Cincinnati, OH (United States). Dept. of Chemistry
  4. Louisiana State Univ., Baton Rouge, LA (United States). Dept. of Biological Sciences and Center for Computation and Technology
Publication Date:
Research Org.:
Louisiana State Univ., Baton Rouge, LA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH)
OSTI Identifier:
1356192
Grant/Contract Number:  
FG02-98ER20310; RR019900; GM58843
Resource Type:
Accepted Manuscript
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Volume: 111; Journal Issue: 45; Journal ID: ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; photosynthesis; Photosystem II; PsbP; PsbQ; mass spectrometry

Citation Formats

Mummadisetti, Manjula P., Frankel, Laurie K., Bellamy, Henry D., Sallans, Larry, Goettert, Jost S., Brylinski, Michal, Limbach, Patrick A., and Bricker, Terry M. Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II. United States: N. p., 2014. Web. doi:10.1073/pnas.1415165111.
Mummadisetti, Manjula P., Frankel, Laurie K., Bellamy, Henry D., Sallans, Larry, Goettert, Jost S., Brylinski, Michal, Limbach, Patrick A., & Bricker, Terry M. Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II. United States. https://doi.org/10.1073/pnas.1415165111
Mummadisetti, Manjula P., Frankel, Laurie K., Bellamy, Henry D., Sallans, Larry, Goettert, Jost S., Brylinski, Michal, Limbach, Patrick A., and Bricker, Terry M. Mon . "Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II". United States. https://doi.org/10.1073/pnas.1415165111. https://www.osti.gov/servlets/purl/1356192.
@article{osti_1356192,
title = {Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II},
author = {Mummadisetti, Manjula P. and Frankel, Laurie K. and Bellamy, Henry D. and Sallans, Larry and Goettert, Jost S. and Brylinski, Michal and Limbach, Patrick A. and Bricker, Terry M.},
abstractNote = {We used protein cross-linking and radiolytic footprinting coupled with high-resolution mass spectrometry to examine the structure of PsbP and PsbQ when they are bound to Photosystem II, in this paper. 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 (90K–107V), 93Y and 96K, are in close proximity (≤11.4 Å) to the N-terminal 1E residue of PsbQ. Our 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. Furthermore, 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. Finally, 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.},
doi = {10.1073/pnas.1415165111},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 45,
volume = 111,
place = {United States},
year = {Mon Oct 27 00:00:00 EDT 2014},
month = {Mon Oct 27 00:00:00 EDT 2014}
}

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