메뉴 건너뛰기




Volumn 1, Issue 5, 2016, Pages

Biochemical characterization of Middle East respiratory syndrome coronavirus helicase

Author keywords

ATP hydrolysis; Coronavirus; DNA; Enzyme kinetics; Helicase; RNA

Indexed keywords


EID: 85021799220     PISSN: None     EISSN: 23795042     Source Type: Journal    
DOI: 10.1128/mSphere.00235-16     Document Type: Article
Times cited : (56)

References (43)
  • 1
    • 84903978961 scopus 로고    scopus 로고
    • Evaluation of SSYA10-001 as a replication inhibitor of severe acute respiratory syndrome, mouse hepatitis, and Middle East respiratory syndrome coronaviruses
    • Adedeji AO, Singh K, Kassim A, Coleman CM, Elliott R, Weiss SR, Frieman MB, Sarafianos SG. 2014. Evaluation of SSYA10-001 as a replication inhibitor of severe acute respiratory syndrome, mouse hepatitis, and Middle East respiratory syndrome coronaviruses. Antimicrob Agents Chemother 58:4894-4898. http://dx.doi.org/10.1128/ AAC.02994-14
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 4894-4898
    • Adedeji, A.O.1    Singh, K.2    Kassim, A.3    Coleman, C.M.4    Elliott, R.5    Weiss, S.R.6    Frieman, M.B.7    Sarafianos, S.G.8
  • 5
    • 84901003129 scopus 로고    scopus 로고
    • Current advancements and potential strategies in the development of MERS-CoV vaccines
    • Zhang N, Jiang S, Du L. 2014. Current advancements and potential strategies in the development of MERS-CoV vaccines. Expert Rev Vaccines 13:761-774. http://dx.doi.org/10.1586/14760584.2014.912134
    • (2014) Expert Rev Vaccines , vol.13 , pp. 761-774
    • Zhang, N.1    Jiang, S.2    Du, L.3
  • 6
    • 84941413167 scopus 로고    scopus 로고
    • Middle East respiratory syndrome
    • Zumla A, Hui DS, Perlman S. 2015. Middle East respiratory syndrome. Lancet 386:995-1007. http://dx.doi.org/10.1016/S0140-6736(15)60454-8
    • (2015) Lancet , vol.386 , pp. 995-1007
    • Zumla, A.1    Hui, D.S.2    Perlman, S.3
  • 7
    • 84939231634 scopus 로고    scopus 로고
    • Ligand-induced dimerization of Middle East respiratory syndrome (MERS) coronavirus nsp5 protease (3CLpro): implications for nsp5 regulation and the development of antivirals
    • Tomar S, Johnston ML, St John SE, Osswald HL, Nyalapatla PR, Paul LN, Ghosh AK, Denison MR, Mesecar AD. 2015. Ligand-induced dimerization of Middle East respiratory syndrome (MERS) coronavirus nsp5 protease (3CLpro): implications for nsp5 regulation and the development of antivirals. J Biol Chem 290:19403-19422. http://dx.doi.org/ 10.1074/jbc.M115.651463
    • (2015) J Biol Chem , vol.290 , pp. 19403-19422
    • Tomar, S.1    Johnston, M.L.2    St John, S.E.3    Osswald, H.L.4    Nyalapatla, P.R.5    Paul, L.N.6    Ghosh, A.K.7    Denison, M.R.8    Mesecar, A.D.9
  • 8
    • 84918528852 scopus 로고    scopus 로고
    • Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression
    • Bailey-Elkin BA, Knaap RC, Johnson GG, Dalebout TJ, Ninaber DK, van Kasteren PB, Bredenbeek PJ, Snijder EJ, Kikkert M, Mark BL. 2014. Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression. J Biol Chem 289:34667-34682. http:// dx.doi.org/10.1074/jbc.M114.609644
    • (2014) J Biol Chem , vol.289 , pp. 34667-34682
    • Bailey-Elkin, B.A.1    Knaap, R.C.2    Johnson, G.G.3    Dalebout, T.J.4    Ninaber, D.K.5    van Kasteren, P.B.6    Bredenbeek, P.J.7    Snijder, E.J.8    Kikkert, M.9    Mark, B.L.10
  • 9
    • 44449098281 scopus 로고    scopus 로고
    • SARS-coronavirus replication/ transcription complexes are membrane-protected and need a host factor for activity in vitro
    • Van Hemert MJ, van den Worm SH, Knoops K, Mommaas AM, Gorbalenya AE, Snijder EJ. 2008. SARS-coronavirus replication/ transcription complexes are membrane-protected and need a host factor for activity in vitro. PLoS Pathog 4:e1000054. http://dx.doi.org/ 10.1371/journal.ppat.1000054
    • (2008) PLoS Pathog , vol.4
    • Van Hemert, M.J.1    van den Worm, S.H.2    Knoops, K.3    Mommaas, A.M.4    Gorbalenya, A.E.5    Snijder, E.J.6
  • 10
    • 0026597376 scopus 로고
    • Escherichia coli DNA helicases: mechanisms of DNA unwinding
    • Lohman TM. 1992. Escherichia coli DNA helicases: mechanisms of DNA unwinding. Mol Microbiol 6:5-14. http://dx.doi.org/10.1111/j.1365-2958.1992.tb00831.x
    • (1992) Mol Microbiol , vol.6 , pp. 5-14
    • Lohman, T.M.1
  • 11
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel SS, Picha KM. 2000. Structure and function of hexameric helicases. Annu Rev Biochem 69:651-697. http://dx.doi.org/10.1146/ annurev.biochem.69.1.651
    • (2000) Annu Rev Biochem , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 12
    • 33745823112 scopus 로고    scopus 로고
    • Mechanisms of helicases
    • Patel SS, Donmez I. 2006. Mechanisms of helicases. J Biol Chem 281: 18265-18268. http://dx.doi.org/10.1074/jbc.R600008200
    • (2006) J Biol Chem , vol.281 , pp. 18265-18268
    • Patel, S.S.1    Donmez, I.2
  • 13
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman TM, Bjornson KP. 1996. Mechanisms of helicase-catalyzed DNA unwinding. Annu Rev Biochem 65:169-214. http://dx.doi.org/ 10.1146/annurev.bi.65.070196.001125
    • (1996) Annu Rev Biochem , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 14
    • 0019363395 scopus 로고
    • Proteins controlling the helical structure of DNA
    • Geider K, Hoffmann-Berling H. 1981. Proteins controlling the helical structure of DNA. Annu Rev Biochem 50:233-260. http://dx.doi.org/ 10.1146/annurev.bi.50.070181.001313
    • (1981) Annu Rev Biochem , vol.50 , pp. 233-260
    • Geider, K.1    Hoffmann-Berling, H.2
  • 16
    • 0027518667 scopus 로고
    • Helicase-catalyzed DNA unwinding
    • Lohman TM. 1993. Helicase-catalyzed DNA unwinding. J Biol Chem 268:2269-2272
    • (1993) J Biol Chem , vol.268 , pp. 2269-2272
    • Lohman, T.M.1
  • 17
    • 5344260388 scopus 로고    scopus 로고
    • The RNA helicase, nucleotide 5=-triphosphatase, and RNA 5=-triphosphatase activities of dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core
    • Benarroch D, Selisko B, Locatelli GA, Maga G, Romette JL, Canard B. 2004. The RNA helicase, nucleotide 5=-triphosphatase, and RNA 5=-triphosphatase activities of dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core. Virology 328:208-218. http://dx.doi.org/10.1016/ j.virol.2004.07.004
    • (2004) Virology , vol.328 , pp. 208-218
    • Benarroch, D.1    Selisko, B.2    Locatelli, G.A.3    Maga, G.4    Romette, J.L.5    Canard, B.6
  • 18
    • 25144500083 scopus 로고    scopus 로고
    • A fork-clearing role for UvrD
    • Florés MJ, Sanchez N, Michel B. 2005. A fork-clearing role for UvrD. Mol Microbiol 57:1664-1675. http://dx.doi.org/10.1111/j.1365-2958.2005.04753.x
    • (2005) Mol Microbiol , vol.57 , pp. 1664-1675
    • Florés, M.J.1    Sanchez, N.2    Michel, B.3
  • 19
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • Veaute X, Jeusset J, Soustelle C, Kowalczykowski SC, Le Cam E, Fabre F. 2003. The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments. Nature 423:309-312. http://dx.doi.org/ 10.1038/nature01585
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Le Cam, E.5    Fabre, F.6
  • 20
    • 13244252309 scopus 로고    scopus 로고
    • UvrD helicase, unlike rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli
    • Veaute X, Delmas S, Selva M, Jeusset J, Le Cam E, Matic I, Fabre F, Petit MA. 2005. UvrD helicase, unlike rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli. EMBO J 24:180-189. http:// dx.doi.org/10.1038/sj.emboj.7600485
    • (2005) EMBO J , vol.24 , pp. 180-189
    • Veaute, X.1    Delmas, S.2    Selva, M.3    Jeusset, J.4    Le Cam, E.5    Matic, I.6    Fabre, F.7    Petit, M.A.8
  • 21
    • 34548061530 scopus 로고    scopus 로고
    • UvrD controls the access of recombination proteins to blocked replication forks
    • Lestini R, Michel B. 2007. UvrD controls the access of recombination proteins to blocked replication forks. EMBO J 26:3804-3814. http:// dx.doi.org/10.1038/sj.emboj.7601804
    • (2007) EMBO J , vol.26 , pp. 3804-3814
    • Lestini, R.1    Michel, B.2
  • 22
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an RNA-protein interaction by a DExH/D RNA helicase
    • Jankowsky E, Gross CH, Shuman S, Pyle AM. 2001. Active disruption of an RNA-protein interaction by a DExH/D RNA helicase. Science 291: 121-125. http://dx.doi.org/10.1126/science.291.5501.121
    • (2001) Science , vol.291 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 23
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O, Banroques J, Tanner NK, Linder P. 2006. The DEAD-box protein family of RNA helicases. Gene 367:17-37. http://dx.doi.org/ 10.1016/j.gene.2005.10.019
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 24
    • 84938793067 scopus 로고    scopus 로고
    • Human enterovirus nonstructural protein 2CATPase functions as both an RNA helicase and ATPindependent RNA chaperone
    • Xia H, Wang P, Wang GC, Yang J, Sun X, Wu W, Qiu Y, Shu T, Zhao X, Yin L, Qin CF, Hu Y, Zhou X. 2015. Human enterovirus nonstructural protein 2CATPase functions as both an RNA helicase and ATPindependent RNA chaperone. PLoS Pathog 11:e1005067. http:// dx.doi.org/10.1371/journal.ppat.1005067
    • (2015) PLoS Pathog , vol.11
    • Xia, H.1    Wang, P.2    Wang, G.C.3    Yang, J.4    Sun, X.5    Wu, W.6    Qiu, Y.7    Shu, T.8    Zhao, X.9    Yin, L.10    Qin, C.F.11    Hu, Y.12    Zhou, X.13
  • 28
    • 0742288051 scopus 로고    scopus 로고
    • WRN helicase and FEN-1 form a complex upon replication arrest and together process branchmigrating DNA structures associated with the replication fork
    • Sharma S, Otterlei M, Sommers JA, Driscoll HC, Dianov GL, Kao HI, Bambara RA, Brosh RM, Jr. 2004. WRN helicase and FEN-1 form a complex upon replication arrest and together process branchmigrating DNA structures associated with the replication fork. Mol Biol Cell 15: 734-750. http://dx.doi.org/10.1091/mbc.E03-08-0567
    • (2004) Mol Biol Cell , vol.15 , pp. 734-750
    • Sharma, S.1    Otterlei, M.2    Sommers, J.A.3    Driscoll, H.C.4    Dianov, G.L.5    Kao, H.I.6    Bambara, R.A.7    Brosh, R.M.8
  • 29
    • 2442679084 scopus 로고    scopus 로고
    • Multiple enzymatic activities associated with severe acute respi-ratory syndrome coronavirus helicase
    • Ivanov KA, Thiel V, Dobbe JC, van der Meer Y, Snijder EJ, Ziebuhr J. 2004. Multiple enzymatic activities associated with severe acute respi-ratory syndrome coronavirus helicase. J Virol 78:5619-5632. http:// dx.doi.org/10.1128/JVI.78.11.5619-5632.2004
    • (2004) J Virol , vol.78 , pp. 5619-5632
    • Ivanov, K.A.1    Thiel, V.2    Dobbe, J.C.3    van der Meer, Y.4    Snijder, E.J.5    Ziebuhr, J.6
  • 30
    • 0141960168 scopus 로고    scopus 로고
    • The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5= to 3= viral helicases
    • Tanner JA, Watt RM, Chai YB, Lu LY, Lin MC, Peiris JS, Poon LL, Kung HF, Huang JD. 2003. The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5= to 3= viral helicases. J Biol Chem 278:39578-39582. http://dx.doi.org/10.1074/ jbc.C300328200
    • (2003) J Biol Chem , vol.278 , pp. 39578-39582
    • Tanner, J.A.1    Watt, R.M.2    Chai, Y.B.3    Lu, L.Y.4    Lin, M.C.5    Peiris, J.S.6    Poon, L.L.7    Kung, H.F.8    Huang, J.D.9
  • 32
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ. 1982. Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1:945-951
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 33
    • 0026726096 scopus 로고
    • A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3= to 5= direction
    • Lee CG, Hurwitz J. 1992. A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3= to 5= direction. J Biol Chem 267:4398-4407
    • (1992) J Biol Chem , vol.267 , pp. 4398-4407
    • Lee, C.G.1    Hurwitz, J.2
  • 34
    • 0035918241 scopus 로고    scopus 로고
    • Further characterization of the helicase activity of eIF4A. Substrate specificity
    • Rogers GW, Jr, Lima WF, Merrick WC. 2001. Further characterization of the helicase activity of eIF4A. Substrate specificity. J Biol Chem 276: 12598-12608. http://dx.doi.org/10.1074/jbc.M007560200
    • (2001) J Biol Chem , vol.276 , pp. 12598-12608
    • Rogers, G.W.1    Lima, W.F.2    Merrick, W.C.3
  • 35
    • 0028872259 scopus 로고
    • Pestivirus NS3 (p80) protein possesses RNA helicase activity
    • Warrener P, Collett MS. 1995. Pestivirus NS3 (p80) protein possesses RNA helicase activity. J Virol 69:1720-1726
    • (1995) J Virol , vol.69 , pp. 1720-1726
    • Warrener, P.1    Collett, M.S.2
  • 36
    • 0026452283 scopus 로고
    • DNA substrate specificity of DNA helicase E from calf thymus
    • Turchi JJ, Murante RS, Bambara RA. 1992. DNA substrate specificity of DNA helicase E from calf thymus. Nucleic Acids Res 20:6075-6080. http://dx.doi.org/10.1093/nar/20.22.6075
    • (1992) Nucleic Acids Res , vol.20 , pp. 6075-6080
    • Turchi, J.J.1    Murante, R.S.2    Bambara, R.A.3
  • 38
    • 0033941814 scopus 로고    scopus 로고
    • The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5=-to-3= polarity
    • Seybert A, Hegyi A, Siddell SG, Ziebuhr J. 2000. The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5=-to-3= polarity. RNA 6:1056-1068. http://dx.doi.org/ 10.1017/S1355838200000728
    • (2000) RNA , vol.6 , pp. 1056-1068
    • Seybert, A.1    Hegyi, A.2    Siddell, S.G.3    Ziebuhr, J.4
  • 39
    • 0036374953 scopus 로고    scopus 로고
    • Functional properties of the predicted helicase of porcine reproductive and respiratory syndrome virus
    • Bautista EM, Faaberg KS, Mickelson D, McGruder ED. 2002. Functional properties of the predicted helicase of porcine reproductive and respiratory syndrome virus. Virology 298:258-270. http://dx.doi.org/ 10.1006/viro.2002.1495
    • (2002) Virology , vol.298 , pp. 258-270
    • Bautista, E.M.1    Faaberg, K.S.2    Mickelson, D.3    McGruder, E.D.4
  • 40
    • 0031000887 scopus 로고    scopus 로고
    • Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells
    • Morgenstern KA, Landro JA, Hsiao K, Lin C, Gu Y, Su MS, Thomson JA. 1997. Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells. J Virol 71:3767-3775
    • (1997) J Virol , vol.71 , pp. 3767-3775
    • Morgenstern, K.A.1    Landro, J.A.2    Hsiao, K.3    Lin, C.4    Gu, Y.5    Su, M.S.6    Thomson, J.A.7
  • 41
    • 0029784485 scopus 로고    scopus 로고
    • A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain
    • Preugschat F, Averett DR, Clarke BE, Porter DJ. 1996. A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain. J Biol Chem 271: 24449-24457. http://dx.doi.org/10.1074/jbc.271.40.24449
    • (1996) J Biol Chem , vol.271 , pp. 24449-24457
    • Preugschat, F.1    Averett, D.R.2    Clarke, B.E.3    Porter, D.J.4
  • 42
    • 84865427975 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus replication inhibitor that interferes with the nucleic acid unwinding of the viral helicase
    • Adedeji AO, Singh K, Calcaterra NE, DeDiego ML, Enjuanes L, Weiss S, Sarafianos SG. 2012. Severe acute respiratory syndrome coronavirus replication inhibitor that interferes with the nucleic acid unwinding of the viral helicase. Antimicrob Agents Chemother 56:4718-4728. http:// dx.doi.org/10.1128/AAC.00957-12
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 4718-4728
    • Adedeji, A.O.1    Singh, K.2    Calcaterra, N.E.3    DeDiego, M.L.4    Enjuanes, L.5    Weiss, S.6    Sarafianos, S.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.