Cited by 5Heat shock proteins researchAdvanced Electron Microscopy Techniques and ApplicationsProtein Structure and Dynamics

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Cryo-EM structure of the diapause chaperone artemin

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Parvate, Amar D., Powell, Samantha M., Brookreson, Jory T., Moser, Trevor H., Novikova, Irina V., Zhou, Mowei, Evans, James E.·2022·Frontiers in Molecular Biosciences

Published version of a preprint

Abstract

The protein artemin acts as both an RNA and protein chaperone and constitutes over 10% of all protein in Artemia cysts during diapause. However, its mechanistic details remain elusive since no high-resolution structure of artemin exists. Here we report the full-length structure of artemin at 2.04 Å resolution. The cryo-EM map contains density for an intramolecular disulfide bond between Cys22-Cys61 and resolves the entire C-terminus extending into the core of the assembled protein cage but in a different configuration than previously hypothesized with molecular modeling. We also provide data supporting the role of C-terminal helix F towards stabilizing the dimer form that is believed to be important for its chaperoning activity. We were able to destabilize this effect by placing a tag at the C-terminus to fully pack the internal cavity and cause limited steric hindrance.

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Research works printed but not linked: 36

  1. Afonine, 2018, New tools for the analysis and validation of cryo-EM maps and atomic models, Acta Crystallogr. D. Struct. Biol., 74, 814, 10.1107/S2059798318009324 · DOI
  2. Benesch, 2009, Collisional activation of protein complexes: Picking up the pieces, J. Am. Soc. Mass Spectrom., 20, 341, 10.1016/j.jasms.2008.11.014 · DOI
  3. Chen, 2003, Molecular characterization of artemin and ferritin from Artemia franciscana, Eur. J. Biochem., 270, 137, 10.1046/j.1432-1033.2003.03373.x · DOI
  4. Clegg, 2009, Two highly diverged New World Artemia species, A. franciscana and A. persimilis, from contrasting hypersaline habitats express a conserved stress protein complement, Comp. Biochem. Physiol. A Mol. Integr. Physiol., 153, 451, 10.1016/j.cbpa.2009.04.613 · DOI
  5. Emsley, 2010, Features and development of coot, Acta Crystallogr. D. Biol. Crystallogr., 66, 486, 10.1107/S0907444910007493 · DOI · Paper page
  6. Graf, 2002, Redox-regulated molecular chaperones, Cell. Mol. Life Sci., 59, 1624, 10.1007/pl00012489 · DOI
  7. Grandori, 2003, Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry [doi: 10.1002/jms.390], J. Mass Spectrom., 38, 11, 10.1002/jms.390 · DOI
  8. Hall, 2012, Do charge state signatures guarantee protein conformations?, J. Am. Soc. Mass Spectrom., 23, 1161, 10.1007/s13361-012-0393-z · DOI
  9. Hassani, 2013, Effect of artemin on structural transition of β-lactoglobulin, Spectrochim. Acta. A Mol. Biomol. Spectrosc., 105, 24, 10.1016/j.saa.2012.12.003 · DOI
  10. Hoffmann, 2004, Identification of a redox-regulated chaperone network, EMBO J., 23, 160, 10.1038/sj.emboj.7600016 · DOI
  11. Hu, 2011, The structural stability and chaperone activity of artemin, a ferritin homologue from diapause-destined Artemia embryos, depend on different cysteine residues, Cell Stress Chaperones, 16, 133, 10.1007/s12192-010-0225-7 · DOI
  12. Kumsta, 2009, Redox-regulated chaperones, Biochemistry, 48, 4666, 10.1021/bi9003556 · DOI
  13. Laganowsky, 2021, Variable-temperature native mass spectrometry for studies of protein folding, stabilities, assembly, and molecular interactions, Annu. Rev. Biophys., 51, 63101121, 10.1146/annurev-biophys-102221-101121 · DOI
  14. MacRae, 2016, Stress tolerance during diapause and quiescence of the brine shrimp, Artemia, Cell Stress Chaperones, 21, 9, 10.1007/s12192-015-0635-7 · DOI
  15. McLuckey, 1992, Principles of collisional activation in analytical mass spectrometry, J. Am. Soc. Mass Spectrom., 3, 599, 10.1016/1044-0305(92)85001-Z · DOI
  16. Mosaddegh, 2018, An inter-subunit disulfide bond of artemin acts as a redox switch for its chaperone-like activity, Cell Stress Chaperones, 23, 685, 10.1007/s12192-018-0880-7 · DOI
  17. Niforou, 2014, Molecular chaperones and proteostasis regulation during redox imbalance, Redox Biol., 2, 323, 10.1016/j.redox.2014.01.017 · DOI · Paper page
  18. Novikova, 2018, Protein structural biology using cell-free platform from wheat germ, Adv. Struct. Chem. Imaging, 4, 13, 10.1186/s40679-018-0062-9 · DOI
  19. Novikova, 2021, Tunable heteroassembly of a plant pseudoenzyme-enzyme complex, ACS Chem. Biol., 16, 2315, 10.1021/acschembio.1c00475 · DOI
  20. Pettersen, 2004, UCSF Chimera--a visualization system for exploratory research and analysis, J. Comput. Chem., 25, 1605, 10.1002/jcc.20084 · DOI
  21. Punjani, 2017, cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination, Nat. Methods, 14, 290, 10.1038/nmeth.4169 · DOI · Paper page
  22. Rasti, 2009, Sequence and structural analysis of artemin based on ferritin: A comparative study, Biochim. Biophys. Acta, 1794, 1407, 10.1016/j.bbapap.2009.05.005 · DOI
  23. Rasti, 2012, Identification of RNA-binding sites in artemin based on docking energy landscapes and molecular dynamics simulation, Iran. J. Biotechnol., 10, 8
  24. Rubinstein, 2015, Alignment of cryo-EM movies of individual particles by optimization of image translations, J. Struct. Biol., 192, 188, 10.1016/j.jsb.2015.08.007 · DOI
  25. Shirzad, 2011, Deletion of extra C-terminal segment and its effect on the function and structure of artemin, Int. J. Biol. Macromol., 49, 311, 10.1016/j.ijbiomac.2011.05.005 · DOI
  26. Slobin, 1980, Eukaryotic elongation factor T and artemin: Two antigenically related proteins which reflect the dormant state of Artemia cysts, brine shrimp, Artemia, 2, 557
  27. Takalloo, Stress-dependent conformational changes of artemin: Effects of heat and oxidant, PLoS One, 15, e0242206, 10.1371/journal.pone.0242206 · DOI
  28. Takalloo, Probing heat and oxidation induced conformational changes of molecular chaperone artemin by excitation-emission fluorescence spectroscopy, J. Photochem. Photobiol. B, 211, 112013, 10.1016/j.jphotobiol.2020.112013 · DOI
  29. Takalloo, 2016, Real-time monitoring of artemin in vivo chaperone activity using luciferase as an intracellular reporter, Arch. Biochem. Biophys., 610, 33, 10.1016/j.abb.2016.09.016 · DOI
  30. Takalloo, 2017, Artemin protects cells and proteins against oxidative and salt stress, Int. J. Biol. Macromol., 95, 618, 10.1016/j.ijbiomac.2016.11.088 · DOI
  31. Terwilliger, 2018, Automated map sharpening by maximization of detail and connectivity, Acta Crystallogr. D. Struct. Biol., 74, 545, 10.1107/S2059798318004655 · DOI
  32. Warner, 2004, Artemin is an RNA-binding protein with high thermal stability and potential RNA chaperone activity, Arch. Biochem. Biophys., 424, 189, 10.1016/j.abb.2004.02.022 · DOI
  33. Webb, 2016, Comparative protein structure modeling using MODELLER, Curr. Protoc. Bioinforma., 54, 5.6.1, 10.1002/cpbi.3 · DOI
  34. Williams, 2018, MolProbity: More and better reference data for improved all-atom structure validation, Protein Sci., 27, 293, 10.1002/pro.3330 · DOI · Paper page
  35. Yip, 2020, Atomic-resolution protein structure determination by cryo-EM, Nature, 587, 157, 10.1038/s41586-020-2833-4 · DOI
  36. Zimmermann, 2018, A completely reimplemented MPI bioinformatics toolkit with a new HHpred server at its core, J. Mol. Biol., 430, 2237, 10.1016/j.jmb.2017.12.007 · DOI · Paper page

Metadata

Authors
Parvate, A. D., Powell, S. M., Brookreson, J. T., Moser, T. H., Novikova, I. V., Zhou, M., & Evans, J. E.
Affiliations
Pacific Northwest National Laboratory (US)
Corresponding author
Evans, James E.
Venue
Frontiers in Molecular Biosciences
Published
2022-11-28
Volume
9
Pages
998562-998562
ISSN
2296-889X (ISSN-L)
OpenAlex
W4310266620
Cited by
5
References
4
Citations by year
2025: 3 · 2024: 2
FWCI
0.41
Type
journal article
Language
en
Open access
Locations
  • Frontiers in Molecular Biosciences (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
Funders
Biological and Environmental Research (74915)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
artemin, diapause, molecular chaperones, protein structure, intramolecular disulfide bond, C-terminal helix, protein dimerization, cysts, protein cages, steric hindrance

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