메뉴 건너뛰기




Volumn 17, Issue 6, 2007, Pages 641-652

The AAA+ superfamily - a myriad of motions

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BINDING PROTEIN; DNA A; DYNEIN ADENOSINE TRIPHOSPHATASE; ENDOPEPTIDASE CLPX; GLYCOPROTEIN E1; NITROGEN REGULATORY PROTEIN; PHAGE SHOCK PROTEIN F; PROTEIN CLPB; PROTEIN P97; PROTEIN RUVBL1; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 36549048006     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2007.09.012     Document Type: Review
Times cited : (83)

References (47)
  • 2
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger J.P., and Berger J.M. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu Rev Biophys Biomol Struct 35 (2006) 93-114
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 3
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines
    • In this paper, the authors constructed single-chain pseudo-hexamers consisting of combinations of active or inactive ClpX subunits. They were able to show, using these constructs, that the ClpX power stroke results from ATP hydrolysis in a single subunit and consequently, for ClpX at least, concerted or sequential ATP hydrolysis is not required to translocate the polypeptide.
    • Martin A., Baker T.A., and Sauer R.T. Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines. Nature 437 (2005) 1115-1120. In this paper, the authors constructed single-chain pseudo-hexamers consisting of combinations of active or inactive ClpX subunits. They were able to show, using these constructs, that the ClpX power stroke results from ATP hydrolysis in a single subunit and consequently, for ClpX at least, concerted or sequential ATP hydrolysis is not required to translocate the polypeptide.
    • (2005) Nature , vol.437 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 4
    • 25844525796 scopus 로고    scopus 로고
    • Cellular functions, mechanism of action, and regulation of FtsH protease
    • Ito K., and Akiyama Y. Cellular functions, mechanism of action, and regulation of FtsH protease. Annu Rev Microbiol 59 (2005) 211-231
    • (2005) Annu Rev Microbiol , vol.59 , pp. 211-231
    • Ito, K.1    Akiyama, Y.2
  • 5
    • 33744552902 scopus 로고    scopus 로고
    • Structure of the whole cytosolic region of ATP-dependent protease FtsH
    • In this and the following paper, the structure of the cytosolic part of FtsH from different thermophiles is reported. The structures are similar, though in one case two, and in the other case three, distinct conformations are observed. They agree in that the protease domain forms a hexamer whereas the AAA+ domains (which all have bound ADP) vary in orientation, suggesting a mechanism whereby threading of the polypeptide into the protease active site can occur.
    • Suno R., Niwa H., Tsuchiya D., Zhang X., Yoshida M., and Morikawa K. Structure of the whole cytosolic region of ATP-dependent protease FtsH. Mol Cell 22 (2006) 575-585. In this and the following paper, the structure of the cytosolic part of FtsH from different thermophiles is reported. The structures are similar, though in one case two, and in the other case three, distinct conformations are observed. They agree in that the protease domain forms a hexamer whereas the AAA+ domains (which all have bound ADP) vary in orientation, suggesting a mechanism whereby threading of the polypeptide into the protease active site can occur.
    • (2006) Mol Cell , vol.22 , pp. 575-585
    • Suno, R.1    Niwa, H.2    Tsuchiya, D.3    Zhang, X.4    Yoshida, M.5    Morikawa, K.6
  • 7
    • 0036054289 scopus 로고    scopus 로고
    • The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 15 Å resolution
    • Krzywda S., Brzozowski A.M., Verma C., Karata K., Ogura T., and Wilkinson A.J. The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 15 Å resolution. Structure 10 (2002) 1073-1083
    • (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
  • 8
    • 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., and Morikawa K. Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8. Structure 10 (2002) 1415-1423
    • (2002) Structure , vol.10 , pp. 1415-1423
    • Niwa, H.1    Tsuchiya, D.2    Makyio, H.3    Yoshida, M.4    Morikawa, K.5
  • 10
    • 13844253945 scopus 로고    scopus 로고
    • Conformational changes of p97 during nucleotide hydrolysis determined by small-angle X-ray scattering
    • x, and ADP states, indicating different shapes, especially with regard to the positioning of the N-domain.
    • x, and ADP states, indicating different shapes, especially with regard to the positioning of the N-domain.
    • (2005) Structure , vol.13 , pp. 183-195
    • Davies, J.M.1    Tsuruta, H.2    May, A.P.3    Weis, W.I.4
  • 11
    • 14644415865 scopus 로고    scopus 로고
    • Nucleotide dependent motion and mechanism of action of p97/VCP
    • 3 and ADP-bound states of p97 were explored using X-ray crystallography. Despite the relatively low resolution of the structures, a description of the relative domain movements between states is given.
    • 3 and ADP-bound states of p97 were explored using X-ray crystallography. Despite the relatively low resolution of the structures, a description of the relative domain movements between states is given.
    • (2005) J Mol Biol , vol.347 , pp. 437-452
    • DeLaBarre, B.1    Brunger, A.T.2
  • 12
    • 33846277910 scopus 로고    scopus 로고
    • Structural insights into the p97-Ufd1-Np14 complex
    • In this paper, using negative stain EM single-particle averaging, the authors show that only one Ufd1-Np14 complex binds per p97 hexamer, and that ubiquitin binds to the Ufd1 part of the adaptor complex.
    • Pye V.E., Beuron F., Keetch C.A., McKeown C., Robinson C.V., Meyer H.H., Zhang Z., and Freemont P.S. Structural insights into the p97-Ufd1-Np14 complex. Proc Natl Acad Sci U S A 104 (2007) 467-472. In this paper, using negative stain EM single-particle averaging, the authors show that only one Ufd1-Np14 complex binds per p97 hexamer, and that ubiquitin binds to the Ufd1 part of the adaptor complex.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 467-472
    • Pye, V.E.1    Beuron, F.2    Keetch, C.A.3    McKeown, C.4    Robinson, C.V.5    Meyer, H.H.6    Zhang, Z.7    Freemont, P.S.8
  • 13
    • 28844446882 scopus 로고    scopus 로고
    • Multifunctional roles of the conserved Arg residues in the second region of homology of p97/valosin-containing protein
    • Wang Q., Song C., Irizarry L., Dai R., Zhang X., and Li C.C. Multifunctional roles of the conserved Arg residues in the second region of homology of p97/valosin-containing protein. J Biol Chem 280 (2005) 40515-40523
    • (2005) J Biol Chem , vol.280 , pp. 40515-40523
    • Wang, Q.1    Song, C.2    Irizarry, L.3    Dai, R.4    Zhang, X.5    Li, C.C.6
  • 14
    • 21744460209 scopus 로고    scopus 로고
    • Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
    • Park S., Isaacson R., Kim H.T., Silver P.A., and Wagner G. Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 13 (2005) 995-1005
    • (2005) Structure , vol.13 , pp. 995-1005
    • Park, S.1    Isaacson, R.2    Kim, H.T.3    Silver, P.A.4    Wagner, G.5
  • 15
    • 34547097772 scopus 로고    scopus 로고
    • Isaacson RL, Pye VE, Simpson P, Meyer HH, Zhang X, Freemont PS, Matthews S: Detailed structural insight into the p97-Npl4-Ufd1 interface. J Biol Chem 2007 [Epub ahead of print].
  • 16
    • 33646582995 scopus 로고    scopus 로고
    • Conformational changes in the AAA ATPase p97-p47 adaptor complex
    • In this paper, the differences in shape of the p97/p47 complex in ADP-bound and AMPNP-bound states are described using cryo-EM single-particle averaging. The complex has a 6:3 stoichiometry with clear differences in the positioning of the N-domains and the p47 adaptor.
    • Beuron F., Dreveny I., Yuan X., Pye V.E., McKeown C., Briggs L.C., Cliff M.J., Kaneko Y., Wallis R., Isaacson R.L., et al. Conformational changes in the AAA ATPase p97-p47 adaptor complex. EMBO J 25 (2006) 1967-1976. In this paper, the differences in shape of the p97/p47 complex in ADP-bound and AMPNP-bound states are described using cryo-EM single-particle averaging. The complex has a 6:3 stoichiometry with clear differences in the positioning of the N-domains and the p47 adaptor.
    • (2006) EMBO J , vol.25 , pp. 1967-1976
    • Beuron, F.1    Dreveny, I.2    Yuan, X.3    Pye, V.E.4    McKeown, C.5    Briggs, L.C.6    Cliff, M.J.7    Kaneko, Y.8    Wallis, R.9    Isaacson, R.L.10
  • 17
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B., Weissman J., and Horwich A. Molecular chaperones and protein quality control. Cell 125 (2006) 443-451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 18
  • 19
    • 27844460608 scopus 로고    scopus 로고
    • Biochemical coupling of the two nucleotide binding domains of ClpB: covalent linkage is not a prerequisite for chaperone activity
    • Beinker P., Schlee S., Auvula R., and Reinstein J. Biochemical coupling of the two nucleotide binding domains of ClpB: covalent linkage is not a prerequisite for chaperone activity. J Biol Chem 280 (2005) 37965-37973
    • (2005) J Biol Chem , vol.280 , pp. 37965-37973
    • Beinker, P.1    Schlee, S.2    Auvula, R.3    Reinstein, J.4
  • 20
    • 33846188909 scopus 로고    scopus 로고
    • Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB
    • In this paper, cryo-EM reconstructions of ClpB in Apo, ADP, and AMPPNP states are described. The ATP state was investigated using a double Walker B mutation that binds but does not hydrolyze ATP. Arguably the most important finding is that ATP is essential for high-affinity substrate binding, and the structural reason for this is described.
    • Lee S., Choi J.M., and Tsai F.T. Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol Cell 25 (2007) 261-271. In this paper, cryo-EM reconstructions of ClpB in Apo, ADP, and AMPPNP states are described. The ATP state was investigated using a double Walker B mutation that binds but does not hydrolyze ATP. Arguably the most important finding is that ATP is essential for high-affinity substrate binding, and the structural reason for this is described.
    • (2007) Mol Cell , vol.25 , pp. 261-271
    • Lee, S.1    Choi, J.M.2    Tsai, F.T.3
  • 22
    • 27144444327 scopus 로고    scopus 로고
    • Structural and mechanistic studies of VPS4 proteins
    • This paper reports that the crystal structure of the AAA+ region of human VPS4B shows a β-domain insert into the α subdomain which is shown to be involved in binding to the adaptor protein LIP5. ATP appears necessary to form higher oligomers, which are then able to bind the adaptors.
    • Scott A., Chung H.Y., Gonciarz-Swiatek M., Hill G.C., Whitby F.G., Gaspar J., Holton J.M., Viswanathan R., Ghaffarian S., Hill C.P., and Sundquist W.I. Structural and mechanistic studies of VPS4 proteins. EMBO J 24 (2005) 3658-3669. This paper reports that the crystal structure of the AAA+ region of human VPS4B shows a β-domain insert into the α subdomain which is shown to be involved in binding to the adaptor protein LIP5. ATP appears necessary to form higher oligomers, which are then able to bind the adaptors.
    • (2005) EMBO J , vol.24 , pp. 3658-3669
    • Scott, A.1    Chung, H.Y.2    Gonciarz-Swiatek, M.3    Hill, G.C.4    Whitby, F.G.5    Gaspar, J.6    Holton, J.M.7    Viswanathan, R.8    Ghaffarian, S.9    Hill, C.P.10    Sundquist, W.I.11
  • 24
    • 33846895023 scopus 로고    scopus 로고
    • Bacterial enhancer-binding proteins: unlocking sigma54-dependent gene transcription
    • Rappas M., Bose D., and Zhang X. Bacterial enhancer-binding proteins: unlocking sigma54-dependent gene transcription. Curr Opin Struct Biol 17 (2007) 110-116
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 110-116
    • Rappas, M.1    Bose, D.2    Zhang, X.3
  • 25
    • 25144472529 scopus 로고    scopus 로고
    • Negative regulation of AAA+ ATPase assembly by two component receiver domains: a transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria
    • Doucleff M., Chen B., Maris A.E., Wemmer D.E., Kondrashkina E., and Nixon B.T. Negative regulation of AAA+ ATPase assembly by two component receiver domains: a transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria. J Mol Biol 353 (2005) 242-255
    • (2005) J Mol Biol , vol.353 , pp. 242-255
    • Doucleff, M.1    Chen, B.2    Maris, A.E.3    Wemmer, D.E.4    Kondrashkina, E.5    Nixon, B.T.6
  • 28
    • 33845919591 scopus 로고    scopus 로고
    • Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activator
    • Joly N., Schumacher J., and Buck M. Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activator. J Biol Chem 281 (2006) 34997-35007
    • (2006) J Biol Chem , vol.281 , pp. 34997-35007
    • Joly, N.1    Schumacher, J.2    Buck, M.3
  • 29
    • 33344469160 scopus 로고    scopus 로고
    • Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF
    • 54 subunit of the RNAP. When ATP is bound changes in the orientation of the linker between β2 and α3 result in destabilization of this conformation.
    • 54 subunit of the RNAP. When ATP is bound changes in the orientation of the linker between β2 and α3 result in destabilization of this conformation.
    • (2006) J Mol Biol , vol.357 , pp. 481-492
    • Rappas, M.1    Schumacher, J.2    Niwa, H.3    Buck, M.4    Zhang, X.5
  • 30
  • 32
    • 34248206721 scopus 로고    scopus 로고
    • Sensor I threonine of the AAA+ ATPase transcriptional activator PspF is involved in coupling nucleotide triphosphate hydrolysis to the restructuring of sigma 54-RNA polymerase
    • Schumacher J., Joly N., Rappas M., Bradley D., Wigneshweraraj S.R., Zhang X., and Buck M. Sensor I threonine of the AAA+ ATPase transcriptional activator PspF is involved in coupling nucleotide triphosphate hydrolysis to the restructuring of sigma 54-RNA polymerase. J Biol Chem 282 (2007) 9825-9833
    • (2007) J Biol Chem , vol.282 , pp. 9825-9833
    • Schumacher, J.1    Joly, N.2    Rappas, M.3    Bradley, D.4    Wigneshweraraj, S.R.5    Zhang, X.6    Buck, M.7
  • 33
    • 33847704586 scopus 로고    scopus 로고
    • A role for the conserved GAFTGA motif of AAA+ transcription activators in sensing promoter DNA conformation
    • Dago A.E., Wigneshweraraj S.R., Buck M., and Morett E. A role for the conserved GAFTGA motif of AAA+ transcription activators in sensing promoter DNA conformation. J Biol Chem 282 (2007) 1087-1097
    • (2007) J Biol Chem , vol.282 , pp. 1087-1097
    • Dago, A.E.1    Wigneshweraraj, S.R.2    Buck, M.3    Morett, E.4
  • 34
    • 33846007717 scopus 로고    scopus 로고
    • Crystal structure of the human AAA+ protein RuvBL1
    • This paper reports that the crystal structure of human RuvBL1 shows, in contrast to the prokaryotic RuvB protein, an extra DNA/RNA-binding domain of unknown function, inserted in the α/β subdomain of the AAA+ core.
    • Matias P.M., Gorynia S., Donner P., and Carrondo M.A. Crystal structure of the human AAA+ protein RuvBL1. J Biol Chem 281 (2006) 38918-38929. This paper reports that the crystal structure of human RuvBL1 shows, in contrast to the prokaryotic RuvB protein, an extra DNA/RNA-binding domain of unknown function, inserted in the α/β subdomain of the AAA+ core.
    • (2006) J Biol Chem , vol.281 , pp. 38918-38929
    • Matias, P.M.1    Gorynia, S.2    Donner, P.3    Carrondo, M.A.4
  • 35
    • 33846286030 scopus 로고    scopus 로고
    • Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex
    • Puri T., Wendler P., Sigala B., Saibil H., and Tsaneva I.R. Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. J Mol Biol 366 (2007) 179-192
    • (2007) J Mol Biol , vol.366 , pp. 179-192
    • Puri, T.1    Wendler, P.2    Sigala, B.3    Saibil, H.4    Tsaneva, I.R.5
  • 36
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: components and dynamics at the replication fork
    • Johnson A., and O'Donnell M. Cellular DNA replicases: components and dynamics at the replication fork. Annu Rev Biochem 74 (2005) 283-315
    • (2005) Annu Rev Biochem , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donnell, M.2
  • 37
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • In this paper, the crystal structure of the papillomavirus E1 helicase in complex with single-stranded DNA shows the DNA in the central pore of the hexameric ring. Observed variations in the orientation of the DNA-binding hairpin lead to the suggestion that the helicase functions in a sequential manner such that, in a complete cycle, each protomer binds, and hydrolyzes, ATP, releases ADP and translocates one nucleotide through the pore.
    • Enemark E.J., and Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 442 (2006) 270-445. In this paper, the crystal structure of the papillomavirus E1 helicase in complex with single-stranded DNA shows the DNA in the central pore of the hexameric ring. Observed variations in the orientation of the DNA-binding hairpin lead to the suggestion that the helicase functions in a sequential manner such that, in a complete cycle, each protomer binds, and hydrolyzes, ATP, releases ADP and translocates one nucleotide through the pore.
    • (2006) Nature , vol.442 , pp. 270-445
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 38
    • 33746860263 scopus 로고    scopus 로고
    • Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
    • 1 symmetry. The bound nucleotide mimics ATP, which is known to be required for selfassembly of DnaA at replication origins. This spiral AAA+ assembly occurs in the replication initiators in all three domains of life.
    • 1 symmetry. The bound nucleotide mimics ATP, which is known to be required for selfassembly of DnaA at replication origins. This spiral AAA+ assembly occurs in the replication initiators in all three domains of life.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 676-683
    • Erzberger, J.P.1    Mott, M.L.2    Berger, J.M.3
  • 40
    • 23044464806 scopus 로고    scopus 로고
    • Crystal structure of the central and C-terminal domain of the sigma(54)-activator ZraR
    • Sallai L., and Tucker P.A. Crystal structure of the central and C-terminal domain of the sigma(54)-activator ZraR. J Struct Biol 151 (2005) 160-170
    • (2005) J Struct Biol , vol.151 , pp. 160-170
    • Sallai, L.1    Tucker, P.A.2
  • 41
    • 33749266161 scopus 로고    scopus 로고
    • Structural studies of the archaeal MCM complex in different functional states
    • Costa A., Pape T., van Heel M., Brick P., Patwardhan A., and Onesti S. Structural studies of the archaeal MCM complex in different functional states. J Struct Biol 156 (2006) 210-219
    • (2006) J Struct Biol , vol.156 , pp. 210-219
    • Costa, A.1    Pape, T.2    van Heel, M.3    Brick, P.4    Patwardhan, A.5    Onesti, S.6
  • 42
    • 33751534800 scopus 로고    scopus 로고
    • The dynein family at a glance
    • Hook P., and Vallee R.B. The dynein family at a glance. J Cell Sci 119 (2006) 4369-4371
    • (2006) J Cell Sci , vol.119 , pp. 4369-4371
    • Hook, P.1    Vallee, R.B.2
  • 43
    • 3242809790 scopus 로고    scopus 로고
    • 25 Angstrom resolution structure of a cytoplasmic dynein motor reveals a seven-member planar ring
    • Samso M., and Koonce M.P. 25 Angstrom resolution structure of a cytoplasmic dynein motor reveals a seven-member planar ring. J Mol Biol 340 (2004) 1059-1072
    • (2004) J Mol Biol , vol.340 , pp. 1059-1072
    • Samso, M.1    Koonce, M.P.2
  • 44
    • 33644957493 scopus 로고    scopus 로고
    • A flexible linkage between the dynein motor and its cargo
    • Meng X., Samso M., and Koonce M.P. A flexible linkage between the dynein motor and its cargo. J Mol Biol 357 (2006) 701-706
    • (2006) J Mol Biol , vol.357 , pp. 701-706
    • Meng, X.1    Samso, M.2    Koonce, M.P.3
  • 45
    • 33845507258 scopus 로고    scopus 로고
    • A structural model reveals energy transduction in dynein
    • In this paper, a structural model of the force generating mechanism of the motor protein dynein is proposed based on recent EM reconstructions and homology models of the different domains.
    • Serohijos A.W., Chen Y., Ding F., Elston T.C., and Dokholyan N.V. A structural model reveals energy transduction in dynein. Proc Natl Acad Sci U S A 103 (2006) 18540-18545. In this paper, a structural model of the force generating mechanism of the motor protein dynein is proposed based on recent EM reconstructions and homology models of the different domains.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18540-18545
    • Serohijos, A.W.1    Chen, Y.2    Ding, F.3    Elston, T.C.4    Dokholyan, N.V.5
  • 47


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.