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Volumn 35, Issue , 2006, Pages 93-114

Evolutionary relationships and structural mechanisms of AAA+ proteins

Author keywords

ATPase; Molecular machines; Motors; Remodeling

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEIN AAA; UNCLASSIFIED DRUG;

EID: 33745041480     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.35.040405.101933     Document Type: Review
Times cited : (629)

References (110)
  • 1
    • 4043175756 scopus 로고    scopus 로고
    • The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2
    • Abbate EA, Berger JM, Botchan MR. 2004. The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2. Genes Dev. 18:1981-96
    • (2004) Genes Dev. , vol.18 , pp. 1981-1996
    • Abbate, E.A.1    Berger, J.M.2    Botchan, M.R.3
  • 2
    • 0034254272 scopus 로고    scopus 로고
    • Roles of multimerization and membrane association in the proteolytic functions of FtsH (HflB)
    • Akiyama Y, Ito K. 2000. Roles of multimerization and membrane association in the proteolytic functions of FtsH (HflB). EMBO J. 19:3888-95
    • (2000) EMBO J. , vol.19 , pp. 3888-3895
    • Akiyama, Y.1    Ito, K.2
  • 4
    • 0344091553 scopus 로고    scopus 로고
    • Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model
    • Beuron F, Flynn TC, Ma J, Kondo H, Zhang X, Freemont PS. 2003. Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model. J. Mol. Biol. 327:619-29
    • (2003) J. Mol. Biol. , vol.327 , pp. 619-629
    • Beuron, F.1    Flynn, T.C.2    Ma, J.3    Kondo, H.4    Zhang, X.5    Freemont, P.S.6
  • 5
    • 0030867609 scopus 로고    scopus 로고
    • Sequence analysis of the AAA protein family
    • Beyer A. 1997. Sequence analysis of the AAA protein family. Protein Sci 6:2043-58
    • (1997) Protein Sci , vol.6 , pp. 2043-2058
    • Beyer, A.1
  • 7
    • 10944235448 scopus 로고    scopus 로고
    • ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication
    • Bowers JL, Randell JC, Chen S, Bell SP. 2004. ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication. Mol. Cell 16:967-78
    • (2004) Mol. Cell , vol.16 , pp. 967-978
    • Bowers, J.L.1    Randell, J.C.2    Chen, S.3    Bell, S.P.4
  • 9
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman GD, O'Donnell M, Kuriyan J. 2004. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429:724-30
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 10
    • 0242573090 scopus 로고    scopus 로고
    • NSF and p97/VCP: Similar at first, different at last
    • Brunger AT, DeLaBarre B. 2003. NSF and p97/VCP: similar at first, different at last. FEBS Lett. 555:126-33
    • (2003) FEBS Lett. , vol.555 , pp. 126-133
    • Brunger, A.T.1    Delabarre, B.2
  • 11
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri F, Duguet M. 1995. A 200-amino acid ATPase module in search of a basic function. Bioessays 17:639-50
    • (1995) Bioessays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 12
    • 13844254122 scopus 로고    scopus 로고
    • Unraveling the early steps of prokaryotic replication
    • Cunningham EL, Berger JM. 2005. Unraveling the early steps of prokaryotic replication. Curr. Opin. Struct. Biol. 15:68-76
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 68-76
    • Cunningham, E.L.1    Berger, J.M.2
  • 14
    • 0038475879 scopus 로고    scopus 로고
    • Reconstitution of the Mcm2-7p heterohexamer, subunit arrangement, and ATP site architecture
    • Davey MJ, Indiani C, O'Donnell M. 2003. Reconstitution of the Mcm2-7p heterohexamer, subunit arrangement, and ATP site architecture. J. Biol. Chem. 278:4491-99
    • (2003) J. Biol. Chem. , vol.278 , pp. 4491-4499
    • Davey, M.J.1    Indiani, C.2    O'Donnell, M.3
  • 16
    • 13844253945 scopus 로고    scopus 로고
    • Conformational changes of p97 during nucleotide hydrolysis determined by small-angle X-ray scattering
    • Davies JM, Tsuruta H, May AP, Weis WI. 2005. Conformational changes of p97 during nucleotide hydrolysis determined by small-angle X-ray scattering. Structure 13:183-95
    • (2005) Structure , vol.13 , pp. 183-195
    • Davies, J.M.1    Tsuruta, H.2    May, A.P.3    Weis, W.I.4
  • 17
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • DeLaBarre B, Brunger AT. 2003. Complete structure of p97/valosin- containing protein reveals communication between nucleotide domains. Nat. Struct. Biol. 10:856-63
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 856-863
    • Delabarre, B.1    Brunger, A.T.2
  • 19
    • 0037010120 scopus 로고    scopus 로고
    • AAA+ proteins and substrate recognition, it all depends on their partner in crime
    • Dougan DA, Mogk A, Zeth K, Turgay K, Bukau B. 2002. AAA+ proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett. 529:6-10
    • (2002) FEBS Lett. , vol.529 , pp. 6-10
    • Dougan, D.A.1    Mogk, A.2    Zeth, K.3    Turgay, K.4    Bukau, B.5
  • 21
    • 0029186099 scopus 로고
    • Subunits of the regulatory complex of the 26S protease
    • Dubiel W, Ferrell K, Rechsteiner M. 1995. Subunits of the regulatory complex of the 26S protease. Mol. Biol. Rep. 21:27-34
    • (1995) Mol. Biol. Rep. , vol.21 , pp. 27-34
    • Dubiel, W.1    Ferrell, K.2    Rechsteiner, M.3
  • 22
    • 0037119995 scopus 로고    scopus 로고
    • The structure of bacterial DnaA: Implications for general mechanisms underlying DNA replication initiation
    • Erzberger JP, Pirruccello MM, Berger JM. 2002. The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 21:4763-73
    • (2002) EMBO J. , vol.21 , pp. 4763-4773
    • Erzberger, J.P.1    Pirruccello, M.M.2    Berger, J.M.3
  • 23
    • 10944257577 scopus 로고    scopus 로고
    • The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin
    • Felczak MM, Kaguni JM. 2004. The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin. J. Biol. Chem. 279:51156-62
    • (2004) J. Biol. Chem. , vol.279 , pp. 51156-51162
    • Felczak, M.M.1    Kaguni, J.M.2
  • 24
    • 0035800571 scopus 로고    scopus 로고
    • Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase
    • Fodje MN, Hansson A, Hansson M, Olsen JG, Gough S, et al. 2001. Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase. J. Mol. Biol. 311:111-22
    • (2001) J. Mol. Biol. , vol.311 , pp. 111-122
    • Fodje, M.N.1    Hansson, A.2    Hansson, M.3    Olsen, J.G.4    Gough, S.5
  • 25
    • 1642343784 scopus 로고    scopus 로고
    • Phylogenetic analysis of AAA proteins
    • Frickey T, Lupas AN. 2004. Phylogenetic analysis of AAA proteins. J. Struct. Biol. 146:2-10
    • (2004) J. Struct. Biol. , vol.146 , pp. 2-10
    • Frickey, T.1    Lupas, A.N.2
  • 26
    • 0035007681 scopus 로고    scopus 로고
    • An AAA family tree
    • Frohlich KU. 2001. An AAA family tree. J. Cell Sci. 114:1601-2
    • (2001) J. Cell Sci. , vol.114 , pp. 1601-1602
    • Frohlich, K.U.1
  • 27
    • 4444226952 scopus 로고    scopus 로고
    • Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
    • Gai D, Zhao R, Li D, Finkielstein CV, Chen XS. 2004. Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell 119:47-60
    • (2004) Cell , vol.119 , pp. 47-60
    • Gai, D.1    Zhao, R.2    Li, D.3    Finkielstein, C.V.4    Chen, X.S.5
  • 28
    • 0005073263 scopus 로고    scopus 로고
    • Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein
    • Garbarino JE, Gibbons IR. 2002. Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein. BMC Genomics 3:18
    • (2002) BMC Genomics , vol.3 , pp. 18
    • Garbarino, J.E.1    Gibbons, I.R.2
  • 30
    • 0035252083 scopus 로고    scopus 로고
    • The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase
    • Gomis-Ruth FX, Moncalian G, Perez-Luque R, Gonzalez A, Cabezon E, et al. 2001. The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase. Nature 409:637-41
    • (2001) Nature , vol.409 , pp. 637-641
    • Gomis-Ruth, F.X.1    Moncalian, G.2    Perez-Luque, R.3    Gonzalez, A.4    Cabezon, E.5
  • 31
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III
    • Guenther B, Onrust R, Sali A, O'Donnell M, Kuriyan J. 1997. Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell 91:335-45
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 32
    • 0035860740 scopus 로고    scopus 로고
    • A unique beta-hairpin protruding from AAA+ ATPase domain of RuvB motor protein is involved in the interaction with RuvA DNA recognition protein for branch migration of Holliday junctions
    • Han YW, Iwasaki H, Miyata T, Mayanagi K, Yamada K, et al. 2001. A unique beta-hairpin protruding from AAA+ ATPase domain of RuvB motor protein is involved in the interaction with RuvA DNA recognition protein for branch migration of Holliday junctions. J. Biol. Chem. 276:35024-28
    • (2001) J. Biol. Chem. , vol.276 , pp. 35024-35028
    • Han, Y.W.1    Iwasaki, H.2    Miyata, T.3    Mayanagi, K.4    Yamada, K.5
  • 34
    • 0037108759 scopus 로고    scopus 로고
    • Three semidominant barley mutants with single amino acid substitutions in the smallest magnesium chelatase subunit form defective AAA+ hexamers
    • Hansson A, Willows RD, Roberts TH, Hansson M. 2002. Three semidominant barley mutants with single amino acid substitutions in the smallest magnesium chelatase subunit form defective AAA+ hexamers. Proc. Natl. Acad. Sci. USA 99:13944-49
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13944-13949
    • Hansson, A.1    Willows, R.D.2    Roberts, T.H.3    Hansson, M.4
  • 35
    • 18344403503 scopus 로고    scopus 로고
    • Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit
    • Hartman JJ, Mahr J, McNally K, Okawa K, Iwamatsu A, et al. 1998. Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit. Cell 93:277-87
    • (1998) Cell , vol.93 , pp. 277-287
    • Hartman, J.J.1    Mahr, J.2    McNally, K.3    Okawa, K.4    Iwamatsu, A.5
  • 36
    • 0033595814 scopus 로고    scopus 로고
    • Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin
    • Hartman JJ, Vale RD. 1999. Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin. Science 286:782-85
    • (1999) Science , vol.286 , pp. 782-785
    • Hartman, J.J.1    Vale, R.D.2
  • 37
    • 0037080611 scopus 로고    scopus 로고
    • Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants
    • Hattendorf DA, Lindquist SL. 2002. Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. EMBO J. 21:12-21
    • (2002) EMBO J. , vol.21 , pp. 12-21
    • Hattendorf, D.A.1    Lindquist, S.L.2
  • 38
    • 0036430301 scopus 로고    scopus 로고
    • Replication factor C from the hyperthermophilic archaeon Pyrococcus abyssi does not need ATP hydrolysis for clamp-loading and contains a functionally conserved RFC PCNA-binding domain
    • Henneke G, Gueguen Y, Flament D, Azam P, Querellou J, et al. 2002. Replication factor C from the hyperthermophilic archaeon Pyrococcus abyssi does not need ATP hydrolysis for clamp-loading and contains a functionally conserved RFC PCNA-binding domain. J. Mol. Biol. 323:795-810
    • (2002) J. Mol. Biol. , vol.323 , pp. 795-810
    • Henneke, G.1    Gueguen, Y.2    Flament, D.3    Azam, P.4    Querellou, J.5
  • 39
    • 0344211512 scopus 로고    scopus 로고
    • Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH
    • Herman C, Prakash S, Lu CZ, Matouschek A, Gross CA. 2003. Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. Mol. Cell 11:659-69
    • (2003) Mol. Cell , vol.11 , pp. 659-669
    • Herman, C.1    Prakash, S.2    Lu, C.Z.3    Matouschek, A.4    Gross, C.A.5
  • 40
    • 21244482459 scopus 로고    scopus 로고
    • Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: Allosteric control of a protein machine
    • Hersch GL, Burton RE, Bolon DN, Baker TA, Sauer RT. 2005. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 121:1017-27
    • (2005) Cell , vol.121 , pp. 1017-1027
    • Hersch, G.L.1    Burton, R.E.2    Bolon, D.N.3    Baker, T.A.4    Sauer, R.T.5
  • 41
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • Hinnerwisch J, Fenton WA, Furtak KJ, Farr GW, Horwich AL. 2005. Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121:1029-41
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 44
    • 25844525796 scopus 로고    scopus 로고
    • Cellular functions, mechanism of action, and regulation of FtsH protease
    • Ito K, Akiyama Y. 2005. Cellular functions, mechanism of action, and regulation of FtsH protease. Annu. Rev. Microbiol. 59:211-31
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 211-231
    • Ito, K.1    Akiyama, Y.2
  • 45
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer LM, Leipe DD, Koonin EV, Aravind L. 2004. Evolutionary history and higher order classification of AAA+ ATPases. J Struct Biol 146:11-31
    • (2004) J Struct Biol , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 46
    • 5144223072 scopus 로고    scopus 로고
    • Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: Implications for the origins of chromosome segregation, cell division and viral capsid packaging
    • Iyer LM, Makarova KS, Koonin EV, Aravind L. 2004. Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging. Nucleic Acids Res. 32:5260-79
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5260-5279
    • Iyer, L.M.1    Makarova, K.S.2    Koonin, E.V.3    Aravind, L.4
  • 48
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III
    • Jeruzalmi D, O'Donnell M, Kuriyan J. 2001. Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Cell 106:429-41
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 49
    • 0035943399 scopus 로고    scopus 로고
    • Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III
    • Jeruzalmi D, Yurieva O, Zhao Y, Young M, Stewart J, et al. 2001. Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III. Cell 106:417-28
    • (2001) Cell , vol.106 , pp. 417-428
    • Jeruzalmi, D.1    Yurieva, O.2    Zhao, Y.3    Young, M.4    Stewart, J.5
  • 50
    • 0031591026 scopus 로고    scopus 로고
    • Escherichia coli DnaA protein: The replication initiator
    • Kaguni JM. 1997. Escherichia coli DnaA protein: the replication initiator. Mol. Cell 7:145-57
    • (1997) Mol. Cell , vol.7 , pp. 145-157
    • Kaguni, J.M.1
  • 51
    • 0035422651 scopus 로고    scopus 로고
    • Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli
    • Kato J, Katayama T. 2001. Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli. EMBO J 20:4253-62
    • (2001) EMBO J , vol.20 , pp. 4253-4262
    • Kato, J.1    Katayama, T.2
  • 52
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
    • Kenniston JA, Baker TA, Fernandez JM, Sauer RT. 2003. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114:511-20
    • (2003) Cell , vol.114 , pp. 511-520
    • Kenniston, J.A.1    Baker, T.A.2    Fernandez, J.M.3    Sauer, R.T.4
  • 53
    • 0036054289 scopus 로고    scopus 로고
    • The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 a resolution
    • Krzywda S, Brzozowski AM, Verma C, Karata K, Ogura T, Wilkinson AJ. 2002. The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution. Structure 10:1073-83
    • (2002) Structure , vol.10 , pp. 1073-1083
    • Krzywda, S.1    Brzozowski, A.M.2    Verma, C.3    Karata, K.4    Ogura, T.5    Wilkinson, A.J.6
  • 54
    • 0027299142 scopus 로고
    • Two complementary approaches to study peroxisome biogenesis in Saccharomyces cerevisiae: Forward and reversed genetics
    • Kunau WH, Beyer A, Franken T, Gotte K, Marzioch M, et al. 1993. Two complementary approaches to study peroxisome biogenesis in Saccharomyces cerevisiae: forward and reversed genetics. Biochimie 75:209-24
    • (1993) Biochimie , vol.75 , pp. 209-224
    • Kunau, W.H.1    Beyer, A.2    Franken, T.3    Gotte, K.4    Marzioch, M.5
  • 55
    • 0034194179 scopus 로고    scopus 로고
    • AAA proteases: Cellular machines for degrading membrane proteins
    • Langer T. 2000. AAA proteases: cellular machines for degrading membrane proteins. Trends Biochem. Sci. 25:247-51
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 247-251
    • Langer, T.1
  • 56
    • 0034063607 scopus 로고    scopus 로고
    • ATPase switches controlling DNA replication initiation
    • Lee DG, Bell SP. 2000. ATPase switches controlling DNA replication initiation. Curr. Opin. Cell Biol. 12:280-85
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 280-285
    • Lee, D.G.1    Bell, S.P.2
  • 57
    • 0142091549 scopus 로고    scopus 로고
    • Regulation of the transcriptional activator NtrC1: Structural studies of the regulatory and AAA+ ATPase domains
    • Lee SY, De La Torre A, Yan D, Kustu S, Nixon BT, Wemmer DE. 2003. Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains. Genes Dev. 17:2552-63
    • (2003) Genes Dev. , vol.17 , pp. 2552-2563
    • Lee, S.Y.1    De La Torre, A.2    Yan, D.3    Kustu, S.4    Nixon, B.T.5    Wemmer, D.E.6
  • 58
    • 0026686760 scopus 로고
    • AFG1, a new member of the SEC18-NSF, PAS1, CDC48-VCP, TBP family of ATPases
    • Lee YJ, Wickner RB. 1992. AFG1, a new member of the SEC18-NSF, PAS1, CDC48-VCP, TBP family of ATPases. Yeast 8:787-90
    • (1992) Yeast , vol.8 , pp. 787-790
    • Lee, Y.J.1    Wickner, R.B.2
  • 59
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • Leipe DD, Koonin EV, Aravind L. 2003. Evolution and classification of P-loop kinases and related proteins. J. Mol. Biol. 333:781-815
    • (2003) J. Mol. Biol. , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 60
    • 4644247731 scopus 로고    scopus 로고
    • STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer
    • Leipe DD, Koonin EV, Aravind L. 2004. STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer. J. Mol. Biol. 343:1-28
    • (2004) J. Mol. Biol. , vol.343 , pp. 1-28
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 61
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe DD, Wolf YI, Koonin EV, Aravind L. 2002. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317:41-72
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 62
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide- sensitive fusion protein
    • Lenzen CU, Steinmann D, Whiteheart SW, Weis WI. 1998. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94:525-36
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 63
    • 0038700763 scopus 로고    scopus 로고
    • Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen
    • Li D, Zhao R, Lilyestrom W, Gai D, Zhang R, et al. 2003. Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen. Nature 423:512-18
    • (2003) Nature , vol.423 , pp. 512-518
    • Li, D.1    Zhao, R.2    Lilyestrom, W.3    Gai, D.4    Zhang, R.5
  • 64
    • 0029048775 scopus 로고
    • ORC and Cdc6p interact and determine the frequency of initiation of DNA replication in the genome
    • Liang C, Weinreich M, Stillman B. 1995. ORC and Cdc6p interact and determine the frequency of initiation of DNA replication in the genome. Cell 81:667-76
    • (1995) Cell , vol.81 , pp. 667-676
    • Liang, C.1    Weinreich, M.2    Stillman, B.3
  • 65
    • 19344377042 scopus 로고    scopus 로고
    • Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation
    • Liou GG, Tanny JC, Kruger RG, Walz T, Moazed D. 2005. Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. Cell 121:515-27
    • (2005) Cell , vol.121 , pp. 515-527
    • Liou, G.G.1    Tanny, J.C.2    Kruger, R.G.3    Walz, T.4    Moazed, D.5
  • 66
    • 0033634866 scopus 로고    scopus 로고
    • Structure and function of Cdc6/Cdc18: Implications for origin recognition and checkpoint control
    • Liu J, Smith CL, DeRyckere D, DeAngelis K, Martin GS, Berger JM. 2000. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 6:637-48
    • (2000) Mol. Cell , vol.6 , pp. 637-648
    • Liu, J.1    Smith, C.L.2    Deryckere, D.3    Deangelis, K.4    Martin, G.S.5    Berger, J.M.6
  • 68
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines
    • Martin A, Baker TA, Sauer RT. 2005. Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines. Nature 437:1115-20
    • (2005) Nature , vol.437 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 69
    • 0036843139 scopus 로고    scopus 로고
    • The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication
    • Messer W. 2002. The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication. FEMS Microbiol. Rev. 26:355-74
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 355-374
    • Messer, W.1
  • 70
    • 0034234223 scopus 로고    scopus 로고
    • Cdc6p modulates the structure and DNA binding activity of the origin recognition complex in vitro
    • Mizushima T, Takahashi N, Stillman B. 2000. Cdc6p modulates the structure and DNA binding activity of the origin recognition complex in vitro. Genes Dev. 14:1631-41
    • (2000) Genes Dev. , vol.14 , pp. 1631-1641
    • Mizushima, T.1    Takahashi, N.2    Stillman, B.3
  • 72
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald AF, Aravind L, Spouge JL, Koonin EV. 1999. AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9:27-43
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 73
    • 0036773132 scopus 로고    scopus 로고
    • Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8
    • Niwa H, Tsuchiya D, Makyio H, Yoshida M, Morikawa K. 2002. Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8. Structure 10:1415-23
    • (2002) Structure , vol.10 , pp. 1415-1423
    • Niwa, H.1    Tsuchiya, D.2    Makyio, H.3    Yoshida, M.4    Morikawa, K.5
  • 74
    • 1642377971 scopus 로고    scopus 로고
    • Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
    • Ogura T, Whiteheart SW, Wilkinson AJ. 2004. Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases. J. Struct. Biol. 146:106-12
    • (2004) J. Struct. Biol. , vol.146 , pp. 106-112
    • Ogura, T.1    Whiteheart, S.W.2    Wilkinson, A.J.3
  • 75
    • 0035876202 scopus 로고    scopus 로고
    • The McrBC restriction endonuclease assembles into a ring structure in the presence of G nucleotides
    • Panne D, Muller SA, Wirtz S, Engel A, Bickle TA. 2001. The McrBC restriction endonuclease assembles into a ring structure in the presence of G nucleotides. EMBO J. 20:3210-17
    • (2001) EMBO J. , vol.20 , pp. 3210-3217
    • Panne, D.1    Muller, S.A.2    Wirtz, S.3    Engel, A.4    Bickle, T.A.5
  • 76
    • 20744457369 scopus 로고    scopus 로고
    • Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase
    • Park E, Rho YM, Koh OJ, Ahn SW, Seong IS, et al. 2005. Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase. J. Biol. Chem. 280:22892-98
    • (2005) J. Biol. Chem. , vol.280 , pp. 22892-22898
    • Park, E.1    Rho, Y.M.2    Koh, O.J.3    Ahn, S.W.4    Seong, I.S.5
  • 78
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • Riedl SJ, Li W, Chao Y, Schwarzenbacher R, Shi Y. 2005. Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 434:926-33
    • (2005) Nature , vol.434 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5
  • 80
    • 18744414494 scopus 로고    scopus 로고
    • Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle
    • Rouiller I, DeLaBarre B, May AP, Weis WI, Brunger AT, et al. 2002. Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle. Nat. Struct. Biol. 9:950-57
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 950-957
    • Rouiller, I.1    Delabarre, B.2    May, A.P.3    Weis, W.I.4    Brunger, A.T.5
  • 81
    • 0037636027 scopus 로고    scopus 로고
    • The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae
    • Rusche LN, Kirchmaier AL, Rine J. 2003. The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae. Annu. Rev. Biochem. 72:481-516
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 481-516
    • Rusche, L.N.1    Kirchmaier, A.L.2    Rine, J.3
  • 82
    • 1642321118 scopus 로고    scopus 로고
    • Design and regulation of the AAA+ microtubule motor dynein
    • Sakato M, King SM. 2004. Design and regulation of the AAA+ microtubule motor dynein. J. Struct. Biol. 146:58-71
    • (2004) J. Struct. Biol. , vol.146 , pp. 58-71
    • Sakato, M.1    King, S.M.2
  • 83
    • 5344269437 scopus 로고    scopus 로고
    • Sculpting the proteome with AAA(+) proteases and disassembly machines
    • Sauer RT, Bolon DN, Burton BM, Burton RE, Flynn JM, et al. 2004. Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell 119:9-18
    • (2004) Cell , vol.119 , pp. 9-18
    • Sauer, R.T.1    Bolon, D.N.2    Burton, B.M.3    Burton, R.E.4    Flynn, J.M.5
  • 84
    • 0023658349 scopus 로고
    • ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome
    • Sekimizu K, Bramhill D, Kornberg A. 1987. ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome. Cell 50:259-65
    • (1987) Cell , vol.50 , pp. 259-265
    • Sekimizu, K.1    Bramhill, D.2    Kornberg, A.3
  • 85
    • 23844481082 scopus 로고    scopus 로고
    • The roles of the residues on the channel beta-hairpin and loop structures of simian virus 40 hexameric helicase
    • Shen J, Gai D, Patrick A, Greenleaf WB, Chen XS. 2005. The roles of the residues on the channel beta-hairpin and loop structures of simian virus 40 hexameric helicase. Proc. Natl. Acad. Sci. USA 102:11248-53
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11248-11253
    • Shen, J.1    Gai, D.2    Patrick, A.3    Greenleaf, W.B.4    Chen, X.S.5
  • 86
    • 1542283751 scopus 로고    scopus 로고
    • Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates
    • Siddiqui SM, Sauer RT, Baker TA. 2004. Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates. Genes Dev. 18:369-74
    • (2004) Genes Dev. , vol.18 , pp. 369-374
    • Siddiqui, S.M.1    Sauer, R.T.2    Baker, T.A.3
  • 88
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton MR, Sawaya MR, Ellenberger T, Wigley DB. 2000. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101:589-600
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 91
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story RM, Steitz TA. 1992. Structure of the recA protein-ADP complex. Nature 355:374-76
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 92
    • 0035038810 scopus 로고    scopus 로고
    • DNA replication-coupled inactivation of DnaA protein in vitro: A role for DnaA arginine-334 of the AAA+ Box VIII motif in ATP hydrolysis
    • Su'etsugu M, Kawakami H, Kurokawa K, Kubota T, Takata M, Katayama T. 2001. DNA replication-coupled inactivation of DnaA protein in vitro: a role for DnaA arginine-334 of the AAA+ Box VIII motif in ATP hydrolysis. Mol. Microbiol. 40:376-86
    • (2001) Mol. Microbiol. , vol.40 , pp. 376-386
    • Su'etsugu, M.1    Kawakami, H.2    Kurokawa, K.3    Kubota, T.4    Takata, M.5    Katayama, T.6
  • 93
    • 14844288292 scopus 로고    scopus 로고
    • Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex
    • Su'etsugu M, Shimuta TR, Ishida T, Kawakami H, Katayama T. 2005. Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex. J. Biol. Chem. 280:6528-36
    • (2005) J. Biol. Chem. , vol.280 , pp. 6528-6536
    • Su'etsugu, M.1    Shimuta, T.R.2    Ishida, T.3    Kawakami, H.4    Katayama, T.5
  • 95
    • 0032483990 scopus 로고    scopus 로고
    • The Orc4p and Orc5p subunits of the Xenopus and human origin recognition complex are related to Orc1p and Cdc6p
    • Tugal T, Zou-Yang XH, Gavin K, Pappin D, Canas B, et al. 1998. The Orc4p and Orc5p subunits of the Xenopus and human origin recognition complex are related to Orc1p and Cdc6p. J. Biol. Chem. 273:32421-29
    • (1998) J. Biol. Chem. , vol.273 , pp. 32421-32429
    • Tugal, T.1    Zou-Yang, X.H.2    Gavin, K.3    Pappin, D.4    Canas, B.5
  • 96
    • 0032881250 scopus 로고    scopus 로고
    • MCM proteins in DNA replication
    • Tye BK. 1999. MCM proteins in DNA replication. Annu. Rev. Biochem. 68:649-86
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 649-686
    • Tye, B.K.1
  • 97
    • 0025885443 scopus 로고
    • Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: Inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth
    • Van Spanning RJ, Wansell CW, De Boer T, Hazelaar MJ, Anazawa H, et al. 1991. Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth. J. Bacteriol. 173:6948-61
    • (1991) J. Bacteriol. , vol.173 , pp. 6948-6961
    • Van Spanning, R.J.1    Wansell, C.W.2    De Boer, T.3    Hazelaar, M.J.4    Anazawa, H.5
  • 98
    • 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. 1:945-51
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 99
    • 7444249512 scopus 로고    scopus 로고
    • Nucleotide-dependent domain motions within rings of the RecA/AAA(+) superfamily
    • Wang J. 2004. Nucleotide-dependent domain motions within rings of the RecA/AAA(+) superfamily. J. Struct. Biol. 148:259-67
    • (2004) J. Struct. Biol. , vol.148 , pp. 259-267
    • Wang, J.1
  • 100
    • 0035096082 scopus 로고    scopus 로고
    • Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism
    • Wang J, Song JJ, Franklin MC, Kamtekar S, Im YJ, et al. 2001. Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. Structure 9:177-84
    • (2001) Structure , vol.9 , pp. 177-184
    • Wang, J.1    Song, J.J.2    Franklin, M.C.3    Kamtekar, S.4    Im, Y.J.5
  • 101
    • 0035184442 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU
    • Wang J, Song JJ, Seong IS, Franklin MC, Kamtekar S, et al. 2001. Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU. Structure 9:1107-16
    • (2001) Structure , vol.9 , pp. 1107-1116
    • Wang, J.1    Song, J.J.2    Seong, I.S.3    Franklin, M.C.4    Kamtekar, S.5
  • 102
    • 0033582262 scopus 로고    scopus 로고
    • The Cdc6p nucleotide-binding motif is required for loading Mem proteins onto chromatin
    • Weinreich M, Liang C, Stillman B. 1999. The Cdc6p nucleotide-binding motif is required for loading Mem proteins onto chromatin. Proc. Natl. Acad. Sci. USA 96:441-46
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 441-446
    • Weinreich, M.1    Liang, C.2    Stillman, B.3
  • 103
    • 0030738592 scopus 로고    scopus 로고
    • The interaction of Ras with GTPase-activating proteins
    • Wittinghofer A, Scheffzek K, Ahmadian MR. 1997. The interaction of Ras with GTPase-activating proteins. FEBS Lett. 410:63-67
    • (1997) FEBS Lett. , vol.410 , pp. 63-67
    • Wittinghofer, A.1    Scheffzek, K.2    Ahmadian, M.R.3
  • 104
    • 0033859666 scopus 로고    scopus 로고
    • An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc
    • Wood MA, McMahon SB, Cole MD. 2000. An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc. Mol. Cell 5:321-30
    • (2000) Mol. Cell , vol.5 , pp. 321-330
    • Wood, M.A.1    McMahon, S.B.2    Cole, M.D.3
  • 105
    • 18644379392 scopus 로고    scopus 로고
    • Crystal structure of the RuvA-RuvB complex: A structural basis for the Holliday junction migrating motor machinery
    • Yamada K, Miyata T, Tsuchiya D, Oyama T, Fujiwara Y, et al. 2002. Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 10:671-81
    • (2002) Mol. Cell , vol.10 , pp. 671-681
    • Yamada, K.1    Miyata, T.2    Tsuchiya, D.3    Oyama, T.4    Fujiwara, Y.5
  • 106
    • 0348010363 scopus 로고    scopus 로고
    • Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis
    • Yamada-Inagawa T, Okuno T, Karata K, Yamanaka K, Ogura T. 2003. Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis. J. Biol. Chem. 278:50182-87
    • (2003) J. Biol. Chem. , vol.278 , pp. 50182-50187
    • Yamada-Inagawa, T.1    Okuno, T.2    Karata, K.3    Yamanaka, K.4    Ogura, T.5
  • 107
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorbabditis elegans
    • Yan N, Chai J, Lee ES, Gu L, Liu Q, et al. 2005. Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorbabditis elegans. Nature 437:831-87
    • (2005) Nature , vol.437 , pp. 831-887
    • Yan, N.1    Chai, J.2    Lee, E.S.3    Gu, L.4    Liu, Q.5
  • 108
    • 0034509609 scopus 로고    scopus 로고
    • Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system
    • Yeo HJ, Savvides SN, Herr AB, Lanka E, Waksman G. 2000. Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system. Mol. Cell 6:1461-72
    • (2000) Mol. Cell , vol.6 , pp. 1461-1472
    • Yeo, H.J.1    Savvides, S.N.2    Herr, A.B.3    Lanka, E.4    Waksman, G.5
  • 109
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu RC, Hanson PI, Jahn R, Brunger AT. 1998. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol. 5:803-11
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 110
    • 0036668640 scopus 로고    scopus 로고
    • The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings
    • Yu X, VanLoock MS, Poplawski A, Kelman Z, Xiang T, et al. 2002. The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings. EMBO Rep. 3:792-97
    • (2002) EMBO Rep. , vol.3 , pp. 792-797
    • Yu, X.1    Vanloock, M.S.2    Poplawski, A.3    Kelman, Z.4    Xiang, T.5


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