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Volumn 85, Issue 2, 2017, Pages 342-353

Probing the structural dynamics of the CRISPR-Cas9 RNA-guided DNA-cleavage system by coarse-grained modeling

Author keywords

Cas9; coarse grained modeling; CRISPR; elastic network model; flexibility; hotspot residue; normal mode analysis; transition pathway

Indexed keywords

AMINO ACID; CAS9 ENDONUCLEASE; CRISPR ASSOCIATED PROTEIN; DNA; ENDONUCLEASE; RNA; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CAS9 ENDONUCLEASE STREPTOCOCCUS PYOGENES; GUIDE RNA; PROTEIN BINDING;

EID: 85008234074     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.25229     Document Type: Article
Times cited : (16)

References (67)
  • 1
    • 84857097177 scopus 로고    scopus 로고
    • RNA-guided genetic silencing systems in bacteria and archaea
    • Wiedenheft B, Sternberg SH, Doudna JA. RNA-guided genetic silencing systems in bacteria and archaea. Nature 2012;482:331–338.
    • (2012) Nature , vol.482 , pp. 331-338
    • Wiedenheft, B.1    Sternberg, S.H.2    Doudna, J.A.3
  • 2
    • 84878936806 scopus 로고    scopus 로고
    • CRISPR-mediated adaptive immune systems in bacteria and archaea
    • Sorek R, Lawrence CM, Wiedenheft B. CRISPR-mediated adaptive immune systems in bacteria and archaea. Annu Rev Biochem 2013;82:237–266.
    • (2013) Annu Rev Biochem , vol.82 , pp. 237-266
    • Sorek, R.1    Lawrence, C.M.2    Wiedenheft, B.3
  • 3
    • 84943160849 scopus 로고    scopus 로고
    • CRISPR-Cas immunity in prokaryotes
    • Marraffini LA. CRISPR-Cas immunity in prokaryotes. Nature 2015;526:55–61.
    • (2015) Nature , vol.526 , pp. 55-61
    • Marraffini, L.A.1
  • 4
    • 84923279931 scopus 로고    scopus 로고
    • The structural biology of CRISPR-Cas systems
    • Jiang F, Doudna JA. The structural biology of CRISPR-Cas systems. Curr Opin Struct Biol 2015;30:100–111.
    • (2015) Curr Opin Struct Biol , vol.30 , pp. 100-111
    • Jiang, F.1    Doudna, J.A.2
  • 7
  • 10
    • 84874608929 scopus 로고    scopus 로고
    • RNA-guided editing of bacterial genomes using CRISPR-Cas systems
    • Jiang W, Bikard D, Cox D, Zhang F, Marraffini LA. RNA-guided editing of bacterial genomes using CRISPR-Cas systems. Nat Biotechnol 2013;31:233–239.
    • (2013) Nat Biotechnol , vol.31 , pp. 233-239
    • Jiang, W.1    Bikard, D.2    Cox, D.3    Zhang, F.4    Marraffini, L.A.5
  • 11
    • 84866859751 scopus 로고    scopus 로고
    • Cas9-crRNA ribonucleoprotein complex mediates specific DNA cleavage for adaptive immunity in bacteria
    • Gasiunas G, Barrangou R, Horvath P, Siksnys V. Cas9-crRNA ribonucleoprotein complex mediates specific DNA cleavage for adaptive immunity in bacteria. Proc Natl Acad Sci USA 2012;109:E2579–E2586.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. E2579-E2586
    • Gasiunas, G.1    Barrangou, R.2    Horvath, P.3    Siksnys, V.4
  • 12
    • 79960554003 scopus 로고    scopus 로고
    • Unification of Cas protein families and a simple scenario for the origin and evolution of CRISPR-Cas systems
    • Makarova KS, Aravind L, Wolf YI, Koonin EV. Unification of Cas protein families and a simple scenario for the origin and evolution of CRISPR-Cas systems. Biol Direct 2011;6:38.
    • (2011) Biol Direct , vol.6 , pp. 38
    • Makarova, K.S.1    Aravind, L.2    Wolf, Y.I.3    Koonin, E.V.4
  • 14
    • 84874687019 scopus 로고    scopus 로고
    • Repurposing CRISPR as an RNA-guided platform for sequence-specific control of gene expression
    • Qi LS, Larson MH, Gilbert LA, Doudna JA, Weissman JS, Arkin AP, Lim WA. Repurposing CRISPR as an RNA-guided platform for sequence-specific control of gene expression. Cell 2013;152:1173–1183.
    • (2013) Cell , vol.152 , pp. 1173-1183
    • Qi, L.S.1    Larson, M.H.2    Gilbert, L.A.3    Doudna, J.A.4    Weissman, J.S.5    Arkin, A.P.6    Lim, W.A.7
  • 16
    • 84884160273 scopus 로고    scopus 로고
    • CAS9 transcriptional activators for target specificity screening and paired nickases for cooperative genome engineering
    • Mali P, Aach J, Stranges PB, Esvelt KM, Moosburner M, Kosuri S, Yang L, Church GM. CAS9 transcriptional activators for target specificity screening and paired nickases for cooperative genome engineering. Nat Biotechnol 2013;31:833–838.
    • (2013) Nat Biotechnol , vol.31 , pp. 833-838
    • Mali, P.1    Aach, J.2    Stranges, P.B.3    Esvelt, K.M.4    Moosburner, M.5    Kosuri, S.6    Yang, L.7    Church, G.M.8
  • 17
    • 84954214717 scopus 로고    scopus 로고
    • Biology and applications of CRISPR systems: harnessing nature's toolbox for genome engineering
    • Wright AV, Nunez JK, Doudna JA. Biology and applications of CRISPR systems: harnessing nature's toolbox for genome engineering. Cell 2016;164:29–44.
    • (2016) Cell , vol.164 , pp. 29-44
    • Wright, A.V.1    Nunez, J.K.2    Doudna, J.A.3
  • 18
    • 84929666410 scopus 로고    scopus 로고
    • Expanding the Biologist's Toolkit with CRISPR-Cas9
    • Sternberg SH, Doudna JA. Expanding the Biologist's Toolkit with CRISPR-Cas9. Mol Cell 2015;58:568–574.
    • (2015) Mol Cell , vol.58 , pp. 568-574
    • Sternberg, S.H.1    Doudna, J.A.2
  • 19
    • 84902096048 scopus 로고    scopus 로고
    • Development and applications of CRISPR-Cas9 for genome engineering
    • Hsu PD, Lander ES, Zhang F. Development and applications of CRISPR-Cas9 for genome engineering. Cell 2014;157:1262–1278.
    • (2014) Cell , vol.157 , pp. 1262-1278
    • Hsu, P.D.1    Lander, E.S.2    Zhang, F.3
  • 20
    • 84904798083 scopus 로고    scopus 로고
    • CRISPR/Cas9 for genome editing: progress, implications and challenges
    • Zhang F, Wen Y, Guo X. CRISPR/Cas9 for genome editing: progress, implications and challenges. Human Mol Genet 2014;23:R40–R46.
    • (2014) Human Mol Genet , vol.23 , pp. R40-R46
    • Zhang, F.1    Wen, Y.2    Guo, X.3
  • 26
    • 84933574487 scopus 로고    scopus 로고
    • STRUCTURAL BIOLOGY. A Cas9-guide RNA complex preorganized for target DNA recognition
    • Jiang F, Zhou K, Ma L, Gressel S, Doudna JA. STRUCTURAL BIOLOGY. A Cas9-guide RNA complex preorganized for target DNA recognition. Science 2015;348:1477–1481.
    • (2015) Science , vol.348 , pp. 1477-1481
    • Jiang, F.1    Zhou, K.2    Ma, L.3    Gressel, S.4    Doudna, J.A.5
  • 28
    • 84908508061 scopus 로고    scopus 로고
    • Structural basis of PAM-dependent target DNA recognition by the Cas9 endonuclease
    • Anders C, Niewoehner O, Duerst A, Jinek M. Structural basis of PAM-dependent target DNA recognition by the Cas9 endonuclease. Nature 2014;513:569–573.
    • (2014) Nature , vol.513 , pp. 569-573
    • Anders, C.1    Niewoehner, O.2    Duerst, A.3    Jinek, M.4
  • 30
    • 84877782955 scopus 로고    scopus 로고
    • A CRISPR/Cas system mediates bacterial innate immune evasion and virulence
    • Sampson TR, Saroj SD, Llewellyn AC, Tzeng YL, Weiss DS. A CRISPR/Cas system mediates bacterial innate immune evasion and virulence. Nature 2013;497:254–257.
    • (2013) Nature , vol.497 , pp. 254-257
    • Sampson, T.R.1    Saroj, S.D.2    Llewellyn, A.C.3    Tzeng, Y.L.4    Weiss, D.S.5
  • 31
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus M, McCammon JA. Molecular dynamics simulations of biomolecules. Nat Struct Biol 2002;9:646–652.
    • (2002) Nat Struct Biol , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 32
    • 84866503271 scopus 로고    scopus 로고
    • Structure-based simulations of the translocation mechanism of the hepatitis C virus NS3 helicase along single-stranded nucleic acid
    • Zheng W, Tekpinar M. Structure-based simulations of the translocation mechanism of the hepatitis C virus NS3 helicase along single-stranded nucleic acid. Biophys J 2012;103:1343–1353.
    • (2012) Biophys J , vol.103 , pp. 1343-1353
    • Zheng, W.1    Tekpinar, M.2
  • 33
    • 84861765128 scopus 로고    scopus 로고
    • Computational studies of molecular machines: the ribosome
    • Sanbonmatsu KY. Computational studies of molecular machines: the ribosome. Curr Opin Struct Biol 2012;22:168–174.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 168-174
    • Sanbonmatsu, K.Y.1
  • 34
    • 64649101249 scopus 로고    scopus 로고
    • Long-timescale molecular dynamics simulations of protein structure and function
    • Klepeis JL, Lindorff-Larsen K, Dror RO, Shaw DE. Long-timescale molecular dynamics simulations of protein structure and function. Curr Opin Struct Biol 2009;19:120–127.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 120-127
    • Klepeis, J.L.1    Lindorff-Larsen, K.2    Dror, R.O.3    Shaw, D.E.4
  • 35
    • 84956760340 scopus 로고    scopus 로고
    • A Biophysical Model of CRISPR/Cas9 Activity for Rational Design of Genome Editing and Gene Regulation
    • Farasat I, Salis HM. A Biophysical Model of CRISPR/Cas9 Activity for Rational Design of Genome Editing and Gene Regulation. PLoS Comput Biol 2016;12:e1004724.
    • (2016) PLoS Comput Biol , vol.12
    • Farasat, I.1    Salis, H.M.2
  • 36
    • 17044393884 scopus 로고    scopus 로고
    • Coarse-grained models for proteins
    • Tozzini V. Coarse-grained models for proteins. Curr Opin Struct Biol 2005;15:144–150.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 144-150
    • Tozzini, V.1
  • 37
    • 79951676668 scopus 로고    scopus 로고
    • Minimalist models for proteins: a comparative analysis
    • Tozzini V. Minimalist models for proteins: a comparative analysis. Q Rev Biophys 2010;43:333–371.
    • (2010) Q Rev Biophys , vol.43 , pp. 333-371
    • Tozzini, V.1
  • 39
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama F, Sanejouand YH. Conformational change of proteins arising from normal mode calculations. Protein Eng 2001;14:1–6.
    • (2001) Protein Eng , vol.14 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.H.2
  • 40
    • 0345687171 scopus 로고    scopus 로고
    • A comparative study of motor-protein motions by using a simple elastic-network model
    • Zheng W, Doniach S. A comparative study of motor-protein motions by using a simple elastic-network model. Proc Natl Acad Sci USA 2003;100:13253–13258.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13253-13258
    • Zheng, W.1    Doniach, S.2
  • 41
    • 0036721233 scopus 로고    scopus 로고
    • Normal mode analysis of macromolecular motions in a database framework: developing mode concentration as a useful classifying statistic
    • Krebs WG, Alexandrov V, Wilson CA, Echols N, Yu H, Gerstein M. Normal mode analysis of macromolecular motions in a database framework: developing mode concentration as a useful classifying statistic. Proteins 2002;48:682–695.
    • (2002) Proteins , vol.48 , pp. 682-695
    • Krebs, W.G.1    Alexandrov, V.2    Wilson, C.A.3    Echols, N.4    Yu, H.5    Gerstein, M.6
  • 42
    • 34248586875 scopus 로고    scopus 로고
    • Toward the mechanism of dynamical couplings and translocation in hepatitis C virus NS3 helicase using elastic network model
    • Zheng W, Liao JC, Brooks BR, Doniach S. Toward the mechanism of dynamical couplings and translocation in hepatitis C virus NS3 helicase using elastic network model. Proteins 2007;67:886–896.
    • (2007) Proteins , vol.67 , pp. 886-896
    • Zheng, W.1    Liao, J.C.2    Brooks, B.R.3    Doniach, S.4
  • 43
    • 4344685227 scopus 로고    scopus 로고
    • Global ribosome motions revealed with elastic network model
    • Wang Y, Rader AJ, Bahar I, Jernigan RL. Global ribosome motions revealed with elastic network model. J Struct Biol 2004;147:302–314.
    • (2004) J Struct Biol , vol.147 , pp. 302-314
    • Wang, Y.1    Rader, A.J.2    Bahar, I.3    Jernigan, R.L.4
  • 44
    • 84951804907 scopus 로고    scopus 로고
    • Ribosome Mechanics Informs about Mechanism
    • Zimmermann MT, Jia K, Jernigan RL. Ribosome Mechanics Informs about Mechanism. J Mol Biol 2016;428:802–810.
    • (2016) J Mol Biol , vol.428 , pp. 802-810
    • Zimmermann, M.T.1    Jia, K.2    Jernigan, R.L.3
  • 45
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • Bahar I, Rader AJ. Coarse-grained normal mode analysis in structural biology. Curr Opin Struct Biol 2005;15:586–592.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 46
    • 33745024278 scopus 로고    scopus 로고
    • Symmetry, form, and shape: guiding principles for robustness in macromolecular machines
    • Tama F, Brooks CL. Symmetry, form, and shape: guiding principles for robustness in macromolecular machines. Annu Rev Biophys Biomol Struct 2006;35:115–133.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 115-133
    • Tama, F.1    Brooks, C.L.2
  • 48
    • 33748469301 scopus 로고    scopus 로고
    • A New Method for Coarse-Grained Elastic Normal-Mode Analysis
    • Lu M, Poon B, Ma J. A New Method for Coarse-Grained Elastic Normal-Mode Analysis. J Chem Theory Comput 2006;2:464–471.
    • (2006) J Chem Theory Comput , vol.2 , pp. 464-471
    • Lu, M.1    Poon, B.2    Ma, J.3
  • 49
    • 68149141470 scopus 로고    scopus 로고
    • Protein elastic network models and the ranges of cooperativity
    • Yang L, Song G, Jernigan RL. Protein elastic network models and the ranges of cooperativity. Proc Natl Acad Sci USA 2009;106:12347–12352.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12347-12352
    • Yang, L.1    Song, G.2    Jernigan, R.L.3
  • 50
    • 79551615831 scopus 로고    scopus 로고
    • Decrypting the sequence of structural events during the gating transition of pentameric ligand-gated ion channels based on an interpolated elastic network model
    • Zheng W, Auerbach A. Decrypting the sequence of structural events during the gating transition of pentameric ligand-gated ion channels based on an interpolated elastic network model. PLoS Comput Biol 2011;7:e1001046.
    • (2011) PLoS Comput Biol , vol.7
    • Zheng, W.1    Auerbach, A.2
  • 51
    • 17044427535 scopus 로고    scopus 로고
    • Network of dynamically important residues in the open/closed transition in polymerases is strongly conserved
    • Zheng W, Brooks BR, Doniach S, Thirumalai D. Network of dynamically important residues in the open/closed transition in polymerases is strongly conserved. Structure 2005;13:565–577.
    • (2005) Structure , vol.13 , pp. 565-577
    • Zheng, W.1    Brooks, B.R.2    Doniach, S.3    Thirumalai, D.4
  • 52
    • 33646742004 scopus 로고    scopus 로고
    • Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations
    • Zheng W, Brooks BR, Thirumalai D. Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations. Proc Natl Acad Sci USA 2006;103:7664–7669.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7664-7669
    • Zheng, W.1    Brooks, B.R.2    Thirumalai, D.3
  • 53
    • 68149163617 scopus 로고    scopus 로고
    • Large-scale evaluation of dynamically important residues in proteins predicted by the perturbation analysis of a coarse-grained elastic model
    • Zheng W, Tekpinar M. Large-scale evaluation of dynamically important residues in proteins predicted by the perturbation analysis of a coarse-grained elastic model. BMC Struct Biol 2009;9:45.
    • (2009) BMC Struct Biol , vol.9 , pp. 45
    • Zheng, W.1    Tekpinar, M.2
  • 54
    • 84965181792 scopus 로고    scopus 로고
    • Probing the structural dynamics of the SNARE recycling machine based on coarse-grained modeling
    • Zheng W. Probing the structural dynamics of the SNARE recycling machine based on coarse-grained modeling. Proteins 2016;84:1055–1066
    • (2016) Proteins , vol.84 , pp. 1055-1066
    • Zheng, W.1
  • 55
    • 84860176470 scopus 로고    scopus 로고
    • Coarse-grained modeling of the structural states and transition underlying the powerstroke of dynein motor domain
    • Zheng W. Coarse-grained modeling of the structural states and transition underlying the powerstroke of dynein motor domain. J Chem Phys 2012;136:155103.
    • (2012) J Chem Phys , vol.136 , pp. 155103
    • Zheng, W.1
  • 56
    • 84947800807 scopus 로고    scopus 로고
    • A combined coarse-grained and all-atom simulation of TRPV1 channel gating and heat activation
    • Zheng W, Qin F. A combined coarse-grained and all-atom simulation of TRPV1 channel gating and heat activation. J Gen Physiol 2015;145:443–456.
    • (2015) J Gen Physiol , vol.145 , pp. 443-456
    • Zheng, W.1    Qin, F.2
  • 57
    • 77955833735 scopus 로고    scopus 로고
    • Predicting order of conformational changes during protein conformational transitions using an interpolated elastic network model
    • Tekpinar M, Zheng W. Predicting order of conformational changes during protein conformational transitions using an interpolated elastic network model. Proteins 2010;78:2469–2481.
    • (2010) Proteins , vol.78 , pp. 2469-2481
    • Tekpinar, M.1    Zheng, W.2
  • 58
    • 67849122319 scopus 로고    scopus 로고
    • Web 3DNA–a web server for the analysis, reconstruction, and visualization of three-dimensional nucleic-acid structures
    • Zheng G, Lu XJ, Olson WK. Web 3DNA–a web server for the analysis, reconstruction, and visualization of three-dimensional nucleic-acid structures. Nucleic Acids Res 2009;37(Web Server issue):W240–W246.
    • (2009) Nucleic Acids Res , vol.37 , Issue.Web Server issue , pp. W240-W246
    • Zheng, G.1    Lu, X.J.2    Olson, W.K.3
  • 59
    • 77949889825 scopus 로고    scopus 로고
    • Multiscale modeling of structural dynamics underlying force generation and product release in actomyosin complex
    • Zheng W. Multiscale modeling of structural dynamics underlying force generation and product release in actomyosin complex. Proteins 2010;78:638–660.
    • (2010) Proteins , vol.78 , pp. 638-660
    • Zheng, W.1
  • 60
    • 84946215320 scopus 로고    scopus 로고
    • Conformational control of DNA target cleavage by CRISPR-Cas9
    • Sternberg SH, LaFrance B, Kaplan M, Doudna JA. Conformational control of DNA target cleavage by CRISPR-Cas9. Nature 2015;527:110–113.
    • (2015) Nature , vol.527 , pp. 110-113
    • Sternberg, S.H.1    LaFrance, B.2    Kaplan, M.3    Doudna, J.A.4
  • 61
    • 20444409186 scopus 로고    scopus 로고
    • Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes
    • Yang LW, Bahar I. Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes. Structure 2005;13:893–904.
    • (2005) Structure , vol.13 , pp. 893-904
    • Yang, L.W.1    Bahar, I.2
  • 62
    • 34548304871 scopus 로고    scopus 로고
    • Protein conformational transitions explored by mixed elastic network models
    • Zheng W, Brooks BR, Hummer G. Protein conformational transitions explored by mixed elastic network models. Proteins 2007;69:43–57.
    • (2007) Proteins , vol.69 , pp. 43-57
    • Zheng, W.1    Brooks, B.R.2    Hummer, G.3
  • 63
    • 84934435974 scopus 로고    scopus 로고
    • Analysis of protein conformational transitions using elastic network model
    • Zheng W, Tekpinar M. Analysis of protein conformational transitions using elastic network model. Methods Mol Biol 2014;1084:159–172.
    • (2014) Methods Mol Biol , vol.1084 , pp. 159-172
    • Zheng, W.1    Tekpinar, M.2
  • 64
    • 84860176470 scopus 로고    scopus 로고
    • Coarse-grained modeling of the structural states and transition underlying the powerstroke of dynein motor domain
    • Zheng W. Coarse-grained modeling of the structural states and transition underlying the powerstroke of dynein motor domain. J Chem Phys 2012;136:155103.
    • (2012) J Chem Phys , vol.136 , pp. 155103
    • Zheng, W.1
  • 65
    • 79958770374 scopus 로고    scopus 로고
    • Coarse-grained modeling of conformational transitions underlying the processive stepping of myosin V dimer along filamentous actin
    • Zheng W. Coarse-grained modeling of conformational transitions underlying the processive stepping of myosin V dimer along filamentous actin. Proteins 2011;79:2291–2305.
    • (2011) Proteins , vol.79 , pp. 2291-2305
    • Zheng, W.1
  • 66
    • 84872614940 scopus 로고    scopus 로고
    • Coarse-grained and all-atom modeling of structural states and transitions in hemoglobin
    • Tekpinar M, Zheng W. Coarse-grained and all-atom modeling of structural states and transitions in hemoglobin. Proteins 2013;81:240–252.
    • (2013) Proteins , vol.81 , pp. 240-252
    • Tekpinar, M.1    Zheng, W.2
  • 67
    • 84991664243 scopus 로고    scopus 로고
    • ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules
    • Ashkenazy H, Abadi S, Martz E, Chay O, Mayrose I, Pupko T, Ben-Tal N. ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules. Nucleic Acids Res 2016;44: W344–W350.
    • (2016) Nucleic Acids Res , vol.44 , pp. W344-W350
    • Ashkenazy, H.1    Abadi, S.2    Martz, E.3    Chay, O.4    Mayrose, I.5    Pupko, T.6    Ben-Tal, N.7


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