Analysis of High-Affinity Binding of Protein Kinase R to Double-Stranded RNA
Open accessAbstract
Protein kinase R (PKR) is an interferon-induced kinase that plays a pivotal role in the innate immunity response to viral infection. PKR is activated upon binding to double-stranded RNA (dsRNA). Our previous analysis of binding of PKR to dsRNAs ranging from 20 to 40 bp supports a dimerization model for activation in which 30 bp represents the minimal length required to bind two PKR monomers and activate PKR via autophosphorylation. These studies were complicated by the formation of protein-RNA aggregates, particularly at low salt concentrations using longer dsRNAs. Here, we have taken advantage of the enhanced sensitivity afforded using fluorescence-detected analytical ultracentrifugation to reduce the RNA concentrations from micromolar to nanomolar. Under these conditions, we are able to characterize high-affinity binding of PKR to longer dsRNAs in 75 mM NaCl. The PKR binding stoichiometries are increased at lower salt concentrations but remain lower than those previously obtained for the dsRNA binding domain. The dependence of the limiting PKR binding stoichiometries on dsRNA length does not conform to standard models for nonspecific binding and suggests that binding to longer sequences occurs via a different binding mode with a larger site size. Although dimerization plays a key role in the PKR activation mechanism, the ability of shorter dsRNAs to bind two PKR monomers is not sufficient to induce autophosphorylation. We propose that activation of PKR by longer RNAs is correlated with an alternative binding mode in which both of the dsRNA binding motifs contact the RNA, inducing PKR to dimerize via a direct interaction of the kinase domains.
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Long double-stranded regions may induce unwanted innate immune responses.
“In addition, it has been revealed that long double-stranded regions may induce unwanted innate immune responses by previous studies27,54,55.”
From Algorithm for optimized mRNA design improves stability and immunogenicity (2023) · cites this paper as [54]
The Abstract identifies PKR as part of the innate immune response and reports that longer dsRNAs can activate it. The Discussion likewise describes activation by longer RNAs, but the paper does not establish that the resulting immune response is unwanted. (LLM, conf=0.84)
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Cites
Schuck, P. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76713-0 · Cited by 3,868 · see citing works
Analytical ultracentrifugation in biochemistry and polymer science
Harding, S. E. (1995) · Analytica Chimica Acta · doi:10.1016/0003-2670(95)90401-8 · Cited by 1,991 · see citing works
Stafford, W. F. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90316-y · Cited by 517 · see citing works
Interactions between Double-Stranded RNA Regulators and the Protein Kinase DAI
Manche, L., Green, S. R., Schmedt, C., & Mathews, M. B. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.5238 · Cited by 484 · see citing works
Ryter, J. M., & Schultz, S. C. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7505 · Cited by 479 · see citing works
Mechanistic Link between PKR Dimerization, Autophosphorylation, and eIF2α Substrate Recognition
Dey, M., Cao, C., Dar, A. C., Tamura, T., Ozato, K., Sicheri, F., & Dever, T. E. (2005) · Cell · doi:10.1016/j.cell.2005.06.041 · Cited by 366 · see citing works
Nanduri, S., Carpick, B. W., Yang, Y., Williams, B. R. G., & Qin, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.18.5458 · Cited by 312 · see citing works
The double-stranded-RNA-binding motif: interference and much more
Tian, B., Bevilacqua, P. C., Diegelman‐Parente, A., & Mathews, M. B. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1528 · Cited by 259 · see citing works
Stafford, W. F., & Sherwood, P. J. (2004) · Biophysical Chemistry · doi:10.1016/j.bpc.2003.10.028 · Cited by 256 · see citing works
Hunter, T. R., Hunt, T., Jackson, R. J., & Robertson, H. D. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41914-5 · Cited by 248 · see citing works
Bevilacqua, P. C., & Cech, T. R. (1996) · Biochemistry · doi:10.1021/bi9607259 · Cited by 227 · see citing works
Inhibition of PKR by RNA and DNA viruses
Langland, J., Cameron, J. M., Heck, M. C., Jancovich, J. K., & Jacobs, B. L. (2006) · Virus Research · doi:10.1016/j.virusres.2005.10.014 · Cited by 222 · see citing works
Philo, J. S. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.04.053 · Cited by 217 · see citing works
Mechanism of PKR Activation by dsRNA
Lemaire, P. A., Anderson, E., Lary, J. W., & Cole, J. L. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.05.056 · Cited by 211 · see citing works
Self-citationCooperative and non-cooperative binding of large ligands to a finite one-dimensional lattice
Epstein, I. R. (1978) · Biophysical Chemistry · doi:10.1016/0301-4622(78)80015-5 · Cited by 201 · see citing works
Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI.
Kostura, M. J., & Mathews, M. B. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1576 · Cited by 190 · see citing works
Activation of PKR: an open and shut case?
COLE, J. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.12.003 · Cited by 153 · see citing works
Self-citationProtein-Nucleic Acid Interactions. II. Oligopeptide-Polyribonucleotide Binding Studies*
Latt, S. A., & Sober, H. A. (1967) · Biochemistry · doi:10.1021/bi00862a040 · Cited by 145 · see citing works
Analysis of Heterogeneous Interactions
Cole, J. L. (2004) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(04)84013-8 · Cited by 144 · see citing works
Self-citationRegulation of innate immunity through RNA structure and the protein kinase PKR
Nallagatla, S. R., Toroney, R., & Bevilacqua, P. C. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.11.003 · Cited by 133 · see citing works
Lemaire, P. A., Lary, J. W., & Cole, J. L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.031 · Cited by 108 · see citing works
Self-citationHigher-Order Substrate Recognition of eIF2α by the RNA-Dependent Protein Kinase PKR
Dar, A., Dever, T., & Sicheri, F. (2005) · Cell · doi:10.1016/j.cell.2005.06.044 · Cited by 107 · see citing works
Schmedt, C., Green, S. R., Manche, L., Taylor, D. R., Ma, Y., & Mathews, M. B. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0278 · Cited by 106 · see citing works
Toth, A. M., Zhang, P., Das, S., George, C. X., & Samuel, C. E. (2006) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(06)81010-x · Cited by 101 · see citing works
The regulation of the protein kinase PKR by RNA
Robertson, H. D., & Mathews, M. B. (1996) · Biochimie · doi:10.1016/s0300-9084(97)86712-0 · Cited by 94 · see citing works
Ucci, J. W., Kobayashi, Y., Choi, G., Alexandrescu, A. T., & Cole, J. L. (2006) · Biochemistry · doi:10.1021/bi061531o · Cited by 66 · see citing works
Self-citationSpanggord, R. J., Vuyisich, M., & Beal, P. A. (2002) · Biochemistry · doi:10.1021/bi0120594 · Cited by 47 · see citing works
Analysis of high-affinity assembly for AMPA receptor amino-terminal domains
Zhao, H., Berger, A. J., Brown, P. H., Kumar, J., Balbo, A., May, C. A., Casillas, E., Laue, T. M., Patterson, G. H., Mayer, M. L., et al. (2012) · The Journal of General Physiology · doi:10.1085/jgp.201210770 · Cited by 45 · see citing works
Global analysis of non-specific protein–nucleic interactions by sedimentation equilibrium
Ucci, J. W., & Cole, J. L. (2004) · Biophysical Chemistry · doi:10.1016/j.bpc.2003.10.033 · Cited by 39 · see citing works
Self-citationHeparin Activates PKR by Inducing Dimerization
Anderson, E., Pierre-Louis, W., Wong, C. J., Lary, J. W., & Cole, J. L. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.09.025 · Cited by 30 · see citing works
Self-citationAnalysis of PKR–RNA Interactions by Sedimentation Velocity
Wong, C. J., Launer-Felty, K., & Cole, J. L. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-381268-1.00003-3 · Cited by 22 · see citing works
Self-citationMunro, P. D., Jackson, C. M., & Winzor, D. J. (2000) · Journal of Theoretical Biology · doi:10.1006/jtbi.2000.1099 · Cited by 18 · see citing works
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Zhang, H., Zhang, L., Lin, A., Xu, C., Li, Z., Liu, K., Liu, B., Ma, X., Zhao, F., Jiang, H., et al. (2023) · Nature · doi:10.1038/s41586-023-06127-z · Cited by 498 · see citing works
Cellular origins of dsRNA, their recognition and consequences
Chen, Y. G., & Hur, S. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00430-1 · Cited by 430 · see citing works
Double-Stranded RNA Sensors and Modulators in Innate Immunity
Hur, S. (2019) · Annual Review of Immunology · doi:10.1146/annurev-immunol-042718-041356 · Cited by 420 · see citing works
Sampey, G. C., Saifuddin, M., Schwab, A., Barclay, R. A., Punya, S., Chung, M., Hakami, R. M., Zadeh, M. A., Lepene, B. S., Klase, Z. A., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.662171 · Cited by 211 · see citing works
Functional peptides for siRNA delivery
Tai, W., & Gao, X. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2016.08.004 · Cited by 198 · see citing works
Immunogenicity of In Vitro -Transcribed RNA
Mu, X. N., & Hur, S. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.1c00521 · Cited by 138 · see citing works
van der Veen, A. G., Maillard, P. V., Schmidt, J. M., Lee, S. A., Deddouche, S., Borg, A., Kjær, S., Snijders, A. P., & Sousa, C. R. E. (2018) · The EMBO Journal · doi:10.15252/embj.201797479 · Cited by 135 · see citing works
Slicing and dicing viruses: antiviral RNA interference in mammals
Maillard, P. V., van der Veen, A. G., Poirier, E. Z., & Sousa, C. R. E. (2019) · The EMBO Journal · doi:10.15252/embj.2018100941 · Cited by 128 · see citing works
Innate immune responses to RNA: sensing and signaling
Luan, X., Wang, L., Song, G., & Zhou, W. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1287940 · Cited by 79 · see citing works
Bou‐Nader, C., Gordon, J. M., Henderson, F. E., & Zhang, J. (2019) · RNA · doi:10.1261/rna.070169.118 · Cited by 67 · see citing works
Zhou, H.-R., He, K., Landgraf, J., Pan, X., & Pestka, J. J. (2014) · Toxins · doi:10.3390/toxins6123406 · Cited by 66 · see citing works
Understanding the impact of in vitro transcription byproducts and contaminants
Lenk, R., Kleindienst, W., Szabó, G. T., Baiersdörfer, M., Boros, G., Keller, J. M., Mahiny, A. J., & Vlatkovic, I. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1426129 · Cited by 63 · see citing works
Temporal control of the integrated stress response by a stochastic molecular switch
Klein, P., Kallenberger, S. M., Roth, H., Roth, K., Ly-Hartig, T. B. N., Magg, V., Aleš, J., Talemi, S. R., Qiang, Y., Wolf, S., et al. (2022) · Science Advances · doi:10.1126/sciadv.abk2022 · Cited by 50 · see citing works
Crystal structure of an adenovirus virus-associated RNA
Hood, I. V., Gordon, J. M., Bou‐Nader, C., Henderson, F. E., Bahmanjah, S., & Zhang, J. (2019) · Nature Communications · doi:10.1038/s41467-019-10752-6 · Cited by 48 · see citing works
Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions
Chaturvedi, S. K., Ma, J., Zhao, H., & Schuck, P. (2017) · Nature Protocols · doi:10.1038/nprot.2017.064 · Cited by 44 · see citing works
Zhan, Q., Song, R., Zeng, Q., Yao, Q., Ao, L., Xu, D., Fullerton, D. A., & Meng, X. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.10905 · Cited by 42 · see citing works
Branscome, H., Paul, S., Khatkar, P., Kim, Y., Barclay, R. A., Pinto, D. O., Yin, D., Zhou, W., Liotta, L. A., El‐Hage, N., et al. (2019) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-019-09865-y · Cited by 37 · see citing works
Zhao, H., Lomash, S., Glasser, C. R., Mayer, M. L., & Schuck, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083439 · Cited by 35 · see citing works
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Lamichhane, P. P., & Samir, P. (2023) · Biology · doi:10.3390/biology12091172 · Cited by 27 · see citing works
Regulation of PKR by RNA: Formation of Active and Inactive Dimers
Husain, B., Hesler, S. J., & Cole, J. L. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b01046 · Cited by 27 · see citing works
Self-citationInteraction of PKR with single-stranded RNA
Mayo, C. B., & Cole, J. L. (2017) · Scientific Reports · doi:10.1038/s41598-017-03047-7 · Cited by 27 · see citing works
Self-citationImpact of the structural integrity of the three-way junction of adenovirus VAI RNA on PKR inhibition
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Launer-Felty, K., & Cole, J. L. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.12.019 · Cited by 19 · see citing works
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Zhao, H., Ma, J., Ingaramo, M., Andrade, E., MacDonald, J., Ramsay, G. D., Piszczek, G., Patterson, G. H., & Schuck, P. (2014) · Analytical Chemistry · doi:10.1021/ac502478a · Cited by 14 · see citing works
Hu, Y., Fan, L., Wu, C., Wang, B., Sun, Z., & Hu, C. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.01.011 · Cited by 10 · see citing works
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Cieslicka, J., Pianka, K., Drążkowska, K., & Sikorski, P. J. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250259 · Cited by 2 · see citing works
Andrews, R. J., & Bass, B. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.08.001 · Cited by 4 · see citing works
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Andrews, R. J., & Bass, B. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.24.634786 · Cited by 1 · see citing works
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(2015) · CRC Press eBooks · doi:10.1201/b19028-12
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Chen, R., He, A., Lindholm, H. T., & Carvalho, D. D. D. (2026) · Nature reviews. Cancer · doi:10.1038/s41568-026-00977-1 · Cited by 1 · see citing works
- Authors
- Husain, B., Mukerji, I., & Cole, J. L.
- Affiliations
- University of Connecticut (US)
- Wesleyan University (US)
- Corresponding author
- Cole, James L.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-10-26
- Volume
- 51
- Issue
- 44
- Pages
- 8764-8770
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- PMC
- PMC3495235
- OpenAlex
- W52630640
- Cited by
- 51
- References
- 32
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 5 · 2023: 3 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 6 · 2018: 1 · 2017: 4 · 2016: 4 · 2015: 7 · 2014: 4 · 2013: 1
- FWCI
- 1.68
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Wesleyan University Digital Collections (Wesleyan University) (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI 53615, R01AI053615)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- PKR, double-stranded RNA, RNA-protein interactions, innate immunity, viral infection, kinase dimerization, autophosphorylation, binding stoichiometry, non-specific binding
- MeSH terms
- Enzyme Activation, Phosphorylation, Protein Binding, RNA, Double-Stranded, Ultracentrifugation, eIF-2 Kinase, Protein Multimerization
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