메뉴 건너뛰기




Volumn 586, Issue 6, 2012, Pages 939-945

Crystal structure of Cmr2 suggests a nucleotide cyclase-related enzyme in type III CRISPR-Cas systems

Author keywords

CRISPR; Nucleotide cyclase; X ray crystallography

Indexed keywords

ADENYLATE CYCLASE; CMR2 PROTEIN; COMPLEMENTARY RNA; DNA POLYMERASE; GUANYLATE CYCLASE; RNA; UNCLASSIFIED DRUG;

EID: 84862822911     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.02.036     Document Type: Article
Times cited : (47)

References (51)
  • 1
    • 79959319829 scopus 로고    scopus 로고
    • CRISPR-based adaptive immune systems
    • Terns, M.P. and Terns, R.M. (2011) CRISPR-based adaptive immune systems. Curr. Opin. Microbiol. 14, 321-327.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 321-327
    • Terns, M.P.1    Terns, R.M.2
  • 2
    • 77249170201 scopus 로고    scopus 로고
    • CRISPR interference. RNA-directed adaptive immunity in bacteria and archaea
    • Marraffini, L.A. and Sontheimer, E.J. (2010) CRISPR interference. RNA-directed adaptive immunity in bacteria and archaea. Nat. Rev. Genet. 11, 181-190.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 181-190
    • Marraffini, L.A.1    Sontheimer, E.J.2
  • 3
    • 77957935381 scopus 로고    scopus 로고
    • CRISPR/Cas system and its role in phage-bacteria interactions
    • Deveau, H., Garneau, J.E. and Moineau, S. (2010) CRISPR/Cas system and its role in phage-bacteria interactions. Annu. Rev. Microbiol. 64, 475-493.
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 475-493
    • Deveau, H.1    Garneau, J.E.2    Moineau, S.3
  • 5
    • 79956157571 scopus 로고    scopus 로고
    • Evolution and classification of the CRISPR-Cas systems
    • Makarova, K.S. et al. (2011) Evolution and classification of the CRISPR-Cas systems. Nat. Rev. Microbiol. 9, 467-477.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 467-477
    • Makarova, K.S.1
  • 6
    • 80755187812 scopus 로고    scopus 로고
    • CRISPR-Cas systems in bacteria and archaea: Versatile small rnas for adaptive defense and regulation
    • Bhaya, D., Davison, M. and Barrangou, R. (2011) CRISPR-Cas systems in bacteria and archaea: versatile small rnas for adaptive defense and regulation. Annu. Rev. Genet. 45, 273-297.
    • (2011) Annu. Rev. Genet. , vol.45 , pp. 273-297
    • Bhaya, D.1    Davison, M.2    Barrangou, R.3
  • 7
    • 15844390228 scopus 로고    scopus 로고
    • CRISPR elements in Yersinia pestis acquire new repeats by preferential uptake of bacteriophage DNA, and provide additional tools for evolutionary studies
    • DOI 10.1099/mic.0.27437-0
    • Pourcel, C., Salvignol, G. and Vergnaud, G. (2005) CRISPR elements in Yersinia pestis acquire new repeats by preferential uptake of bacteriophage DNA, and provide additional tools for evolutionary studies. Microbiology 151, 653-663. (Pubitemid 40425001)
    • (2005) Microbiology , vol.151 , Issue.3 , pp. 653-663
    • Pourcel, C.1    Salvignol, G.2    Vergnaud, G.3
  • 8
    • 16444385662 scopus 로고    scopus 로고
    • Intervening sequences of regularly spaced prokaryotic repeats derive from foreign genetic elements
    • DOI 10.1007/s00239-004-0046-3
    • Mojica, F.J., Diez-Villasenor, C., Garcia-Martinez, J. and Soria, E. (2005) Intervening sequences of regularly spaced prokaryotic repeats derive from foreign genetic elements. J. Mol. Evol. 60, 174-182. (Pubitemid 40568857)
    • (2005) Journal of Molecular Evolution , vol.60 , Issue.2 , pp. 174-182
    • Mojica, F.J.M.1    Diez-Villasenor, C.2    Garcia-Martinez, J.3    Soria, E.4
  • 9
    • 23844505202 scopus 로고    scopus 로고
    • Clustered regularly interspaced short palindrome repeats (CRISPRs) have spacers of extrachromosomal origin
    • DOI 10.1099/mic.0.28048-0
    • Bolotin, A., Quinquis, B., Sorokin, A. and Ehrlich, S.D. (2005) Clustered regularly interspaced short palindrome repeats (CRISPRs) have spacers of extrachromosomal origin. Microbiology 151, 2551-2561. (Pubitemid 41149778)
    • (2005) Microbiology , vol.151 , Issue.8 , pp. 2551-2561
    • Bolotin, A.1    Quinquis, B.2    Sorokin, A.3    Dusko, E.S.4
  • 10
    • 34248374277 scopus 로고    scopus 로고
    • A putative RNA-interference-based immune system in prokaryotes: Computational analysis of the predicted enzymatic machinery, functional analogies with eukaryotic RNAi, and hypothetical mechanisms of action
    • Makarova, K.S., Grishin, N.V., Shabalina, S.A., Wolf, Y.I. and Koonin, E.V. (2006) A putative RNA-interference-based immune system in prokaryotes: computational analysis of the predicted enzymatic machinery, functional analogies with eukaryotic RNAi, and hypothetical mechanisms of action. Biol. Direct. 1, 7.
    • (2006) Biol. Direct. , vol.1 , pp. 7
    • Makarova, K.S.1    Grishin, N.V.2    Shabalina, S.A.3    Wolf, Y.I.4    Koonin, E.V.5
  • 11
    • 34248400310 scopus 로고    scopus 로고
    • A guild of 45 CRISPR-associated (Cas) protein families and multiple CRISPR/Cas subtypes exist in prokaryotic genomes
    • Haft, D.H., Selengut, J., Mongodin, E.F. and Nelson, K.E. (2005) A guild of 45 CRISPR-associated (Cas) protein families and multiple CRISPR/Cas subtypes exist in prokaryotic genomes. PLoS Comput. Biol. 1, e60.
    • (2005) PLoS Comput. Biol. , vol.1
    • Haft, D.H.1    Selengut, J.2    Mongodin, E.F.3    Nelson, K.E.4
  • 12
    • 0036267740 scopus 로고    scopus 로고
    • Identification of genes that are associated with DNA repeats in prokaryotes
    • DOI 10.1046/j.1365-2958.2002.02839.x
    • Jansen, R., Embden, J.D., Gaastra, W. and Schouls, L.M. (2002) Identification of genes that are associated with DNA repeats in prokaryotes. Mol. Microbiol. 43, 1565-1575. (Pubitemid 34595547)
    • (2002) Molecular Microbiology , vol.43 , Issue.6 , pp. 1565-1575
    • Jansen, R.1    Van Embden, J.D.A.2    Gaastra, W..3    Schouls, L.M.4
  • 13
  • 14
    • 66349134987 scopus 로고    scopus 로고
    • Structural basis for DNase activity of a conserved protein implicated in CRISPR-mediated genome defense
    • Wiedenheft, B., Zhou, K., Jinek, M., Coyle, S.M., Ma, W. and Doudna, J.A. (2009) Structural basis for DNase activity of a conserved protein implicated in CRISPR-mediated genome defense. Structure 17, 904-912.
    • (2009) Structure , vol.17 , pp. 904-912
    • Wiedenheft, B.1    Zhou, K.2    Jinek, M.3    Coyle, S.M.4    Ma, W.5    Doudna, J.A.6
  • 15
    • 49649120271 scopus 로고    scopus 로고
    • A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats
    • Beloglazova, N. et al. (2008) A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats. J. Biol. Chem. 283, 20361-20371.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20361-20371
    • Beloglazova, N.1
  • 16
    • 79551694059 scopus 로고    scopus 로고
    • Interaction of the Cas6 Riboendonuclease with CRISPR RNAs: Recognition and cleavage
    • Wang, R., Preamplume, G., Terns, M.P., Terns, R.M. and Li, H. (2011) Interaction of the Cas6 Riboendonuclease with CRISPR RNAs: recognition and cleavage. Structure 19, 257-264.
    • (2011) Structure , vol.19 , pp. 257-264
    • Wang, R.1    Preamplume, G.2    Terns, M.P.3    Terns, R.M.4    Li, H.5
  • 17
    • 79958825675 scopus 로고    scopus 로고
    • An RNA-induced conformational change required for CRISPR RNA cleavage by the endoribonuclease Cse3
    • Sashital, D.G., Jinek, M. and Doudna, J.A. (2011) An RNA-induced conformational change required for CRISPR RNA cleavage by the endoribonuclease Cse3. Nat. Struct. Mol. Biol. 18, 680-687.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 680-687
    • Sashital, D.G.1    Jinek, M.2    Doudna, J.A.3
  • 19
    • 77956498326 scopus 로고    scopus 로고
    • Sequence- and structure-specific RNA processing by a CRISPR endonuclease
    • Haurwitz, R.E., Jinek, M., Wiedenheft, B., Zhou, K. and Doudna, J.A. (2010) Sequence- and structure-specific RNA processing by a CRISPR endonuclease. Science 329, 1355-1358.
    • (2010) Science , vol.329 , pp. 1355-1358
    • Haurwitz, R.E.1    Jinek, M.2    Wiedenheft, B.3    Zhou, K.4    Doudna, J.A.5
  • 20
    • 57049149666 scopus 로고    scopus 로고
    • Prokaryotic silencing (psi)RNAs in Pyrococcus furiosus
    • Hale, C., Kleppe, K., Terns, R.M. and Terns, M.P. (2008) Prokaryotic silencing (psi)RNAs in Pyrococcus furiosus. RNA 14, 2572-2579.
    • (2008) RNA , vol.14 , pp. 2572-2579
    • Hale, C.1    Kleppe, K.2    Terns, R.M.3    Terns, M.P.4
  • 21
    • 58049191229 scopus 로고    scopus 로고
    • Cas6 is an endoribonuclease that generates guide RNAs for invader defense in prokaryotes
    • Carte, J., Wang, R., Li, H., Terns, R.M. and Terns, M.P. (2008) Cas6 is an endoribonuclease that generates guide RNAs for invader defense in prokaryotes. Genes Dev. 22, 3489-3496.
    • (2008) Genes Dev. , vol.22 , pp. 3489-3496
    • Carte, J.1    Wang, R.2    Li, H.3    Terns, R.M.4    Terns, M.P.5
  • 25
    • 57849137502 scopus 로고    scopus 로고
    • CRISPR interference limits horizontal gene transfer in staphylococci by targeting DNA
    • Marraffini, L.A. and Sontheimer, E.J. (2008) CRISPR interference limits horizontal gene transfer in staphylococci by targeting DNA. Science 322, 1843-1845.
    • (2008) Science , vol.322 , pp. 1843-1845
    • Marraffini, L.A.1    Sontheimer, E.J.2
  • 27
    • 79955574254 scopus 로고    scopus 로고
    • Structural basis for CRISPR RNA-guided DNA recognition by Cascade
    • Jore, M.M. et al. (2011) Structural basis for CRISPR RNA-guided DNA recognition by Cascade. Nat. Struct. Mol. Biol. 18, 529-536.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 529-536
    • Jore, M.M.1
  • 28
    • 79953779608 scopus 로고    scopus 로고
    • Cas3 is a single-stranded DNA nuclease and ATP-dependent helicase in the CRISPR/Cas immune system
    • Sinkunas, T., Gasiunas, G., Fremaux, C., Barrangou, R., Horvath, P. and Siksnys, V. (2011) Cas3 is a single-stranded DNA nuclease and ATP-dependent helicase in the CRISPR/Cas immune system. EMBO J. 30, 1335-1342.
    • (2011) EMBO J. , vol.30 , pp. 1335-1342
    • Sinkunas, T.1    Gasiunas, G.2    Fremaux, C.3    Barrangou, R.4    Horvath, P.5    Siksnys, V.6
  • 30
    • 79960554003 scopus 로고    scopus 로고
    • Unification of Cas protein families and a simple scenario for the origin and evolution of CRISPRCas systems
    • Makarova, K.S., Aravind, L., Wolf, Y.I. and Koonin, E.V. (2011) Unification of Cas protein families and a simple scenario for the origin and evolution of CRISPRCas systems. Biol. Direct. 6, 38.
    • (2011) Biol. Direct. , vol.6 , pp. 38
    • Makarova, K.S.1    Aravind, L.2    Wolf, Y.I.3    Koonin, E.V.4
  • 31
    • 0037079680 scopus 로고    scopus 로고
    • A DNA repair system specific for thermophilic Archaea and bacteria predicted by genomic context analysis
    • Makarova, K.S., Aravind, L., Grishin, N.V., Rogozin, I.B. and Koonin, E.V. (2002) A DNA repair system specific for thermophilic Archaea and bacteria predicted by genomic context analysis. Nucleic Acids Res. 30, 482-496. (Pubitemid 34679610)
    • (2002) Nucleic Acids Research , vol.30 , Issue.2 , pp. 482-496
    • Makarova, K.S.1    Aravind, L.2    Grishin, N.V.3    Rogozin, I.B.4    Koonin, E.V.5
  • 32
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • DOI 10.1006/jmbi.1993.1012
    • Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L. and Clardy, J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229, 105-124. (Pubitemid 23037917)
    • (1993) Journal of Molecular Biology , vol.229 , Issue.1 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G.M. (2008) A short history of SHELX. Acta Crystallogr. A 64, 112-122.
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 35
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • DOI 10.1385/1-59745-266-1:215, Macromolecular Crystallography Protocols, Volume 2: Structure Determination
    • Vonrhein, C., Blanc, E., Roversi, P. and Bricogne, G. (2007) Automated structure solution with autoSHARP. Methods Mol. Biol. 364, 215-230. (Pubitemid 350183137)
    • (2007) Methods in Molecular Biology , vol.364 , pp. 215-230
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4
  • 38
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 39
  • 40
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • DOI 10.1006/jmbi.1993.1489
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138. (Pubitemid 23288916)
    • (1993) Journal of Molecular Biology , vol.233 , Issue.1 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 41
    • 0036601353 scopus 로고    scopus 로고
    • Trends in protein evolution inferred from sequence and structure analysis
    • DOI 10.1016/S0959-440X(02)00334-2
    • Aravind, L., Mazumder, R., Vasudevan, S. and Koonin, E.V. (2002) Trends in protein evolution inferred from sequence and structure analysis. Curr. Opin. Struct. Biol. 12, 392-399. (Pubitemid 34804623)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.3 , pp. 392-399
    • Aravind, L.1    Mazumder, R.2    Vasudevan, S.3    Koonin, E.V.4
  • 42
    • 33751438617 scopus 로고    scopus 로고
    • Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases
    • DOI 10.1007/112-0603
    • Sinha, S.C. and Sprang, S.R. (2006) Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases. Rev. Physiol. Biochem. Pharmacol. 157, 105-140. (Pubitemid 44816532)
    • (2006) Reviews of Physiology, Biochemistry and Pharmacology , vol.157 , pp. 105-140
    • Sinha, S.C.1    Sprang, S.R.2
  • 43
    • 0030901637 scopus 로고    scopus 로고
    • Structure of the adenylyl cyclase catalytic core
    • DOI 10.1038/386247a0
    • Zhang, G., Liu, Y., Ruoho, A.E. and Hurley, J.H. (1997) Structure of the adenylyl cyclase catalytic core. Nature 386, 247-253. (Pubitemid 27142504)
    • (1997) Nature , vol.386 , Issue.6622 , pp. 247-253
    • Zhang, G.1    Liu, Y.2    Ruoho, A.E.3    Hurley, J.H.4
  • 44
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with G(salpha).GTPgammaS
    • DOI 10.1126/science.278.5345.1907
    • Tesmer, J.J., Sunahara, R.K., Gilman, A.G. and Sprang, S.R. (1997) Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS. Science 278, 1907-1916. (Pubitemid 28013225)
    • (1997) Science , vol.278 , Issue.5345 , pp. 1907-1916
    • Tesmer, J.J.G.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 45
    • 11444256177 scopus 로고    scopus 로고
    • Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment
    • DOI 10.1038/nsmb880
    • Steegborn, C., Litvin, T.N., Levin, L.R., Buck, J. and Wu, H. (2005) Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment. Nat. Struct. Mol. Biol. 12, 32-37. (Pubitemid 40082914)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.1 , pp. 32-37
    • Steegborn, C.1    Litvin, T.N.2    Levin, L.R.3    Buck, J.4    Wu, H.5
  • 46
    • 66149108791 scopus 로고    scopus 로고
    • X-ray crystal structure of a CRISPR-associated RAMP superfamily protein, Cmr5, from Thermus thermophilus HB8
    • Sakamoto, K., Agari, Y., Agari, K., Yokoyama, S., Kuramitsu, S. and Shinkai, A. (2009) X-ray crystal structure of a CRISPR-associated RAMP superfamily protein, Cmr5, from Thermus thermophilus HB8. Proteins 75, 528-532.
    • (2009) Proteins , vol.75 , pp. 528-532
    • Sakamoto, K.1    Agari, Y.2    Agari, K.3    Yokoyama, S.4    Kuramitsu, S.5    Shinkai, A.6
  • 47
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz, T.A. (1999) DNA polymerases: structural diversity and common mechanisms. J. Biol. Chem. 274, 17395-17398.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 50
    • 34547659282 scopus 로고    scopus 로고
    • --Modified Response Regulator PleD: Implications for Diguanylate Cyclase Activation, Catalysis, and Feedback Inhibition
    • DOI 10.1016/j.str.2007.06.016, PII S0969212607002493
    • Wassmann, P., Chan, C., Paul, R., Beck, A., Heerklotz, H., Jenal, U. and Schirmer, T. (2007) Structure of BeF3- -modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure 15, 915-927. (Pubitemid 47212753)
    • (2007) Structure , vol.15 , Issue.8 , pp. 915-927
    • Wassmann, P.1    Chan, C.2    Paul, R.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6    Schirmer, T.7
  • 51
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • DOI 10.1038/34593
    • Doublie, S., Tabor, S., Long, A.M., Richardson, C.C. and Ellenberger, T. (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution. Nature 391, 251-258. (Pubitemid 28099004)
    • (1998) Nature , vol.391 , Issue.6664 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.