메뉴 건너뛰기




Volumn 47, Issue 3, 2012, Pages 484-490

ATPase Site Architecture Is Required for Self-Assembly and Remodeling Activity of a Hexameric AAA+ Transcriptional Activator

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE ASSOCIATED WITH VARIOUS CELLULAR ACTIVITIES; ADENOSINE TRIPHOSPHATE; ENZYME VARIANT; GLUTAMIC ACID; NUCLEOTIDE; TRANS ACTING FACTOR; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR PSPF; TYROSINE; UNCLASSIFIED DRUG;

EID: 84864911724     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2012.06.012     Document Type: Article
Times cited : (23)

References (30)
  • 1
    • 0031231083 scopus 로고    scopus 로고
    • Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
    • Ahmadian M.R., Stege P., Scheffzek K., Wittinghofer A. Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nat. Struct. Biol. 1997, 4:686-689.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 686-689
    • Ahmadian, M.R.1    Stege, P.2    Scheffzek, K.3    Wittinghofer, A.4
  • 2
    • 4444372098 scopus 로고    scopus 로고
    • Mutational analysis of conserved AAA+ residues in the archaeal Lon protease from Thermoplasma acidophilum
    • Besche H., Tamura N., Tamura T., Zwickl P. Mutational analysis of conserved AAA+ residues in the archaeal Lon protease from Thermoplasma acidophilum. FEBS Lett. 2004, 574:161-166.
    • (2004) FEBS Lett. , vol.574 , pp. 161-166
    • Besche, H.1    Tamura, N.2    Tamura, T.3    Zwickl, P.4
  • 4
    • 0033938884 scopus 로고    scopus 로고
    • Isomerization of a binary sigma-promoter DNA complex by transcription activators
    • Cannon W.V., Gallegos M.T., Buck M. Isomerization of a binary sigma-promoter DNA complex by transcription activators. Nat. Struct. Biol. 2000, 7:594-601.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 594-601
    • Cannon, W.V.1    Gallegos, M.T.2    Buck, M.3
  • 5
    • 78149460165 scopus 로고    scopus 로고
    • Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase
    • Chen B., Sysoeva T.A., Chowdhury S., Guo L., De Carlo S., Hanson J.A., Yang H., Nixon B.T. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure 2010, 18:1420-1430.
    • (2010) Structure , vol.18 , pp. 1420-1430
    • Chen, B.1    Sysoeva, T.A.2    Chowdhury, S.3    Guo, L.4    De Carlo, S.5    Hanson, J.A.6    Yang, H.7    Nixon, B.T.8
  • 6
    • 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 C.V., Chen X.S. Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell 2004, 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
  • 7
    • 44949197849 scopus 로고    scopus 로고
    • Systematic study of the functions for the residues around the nucleotide pocket in simian virus 40 AAA+ hexameric helicase
    • Greenleaf W.B., Shen J., Gai D., Chen X.S. Systematic study of the functions for the residues around the nucleotide pocket in simian virus 40 AAA+ hexameric helicase. J. Virol. 2008, 82:6017-6023.
    • (2008) J. Virol. , vol.82 , pp. 6017-6023
    • Greenleaf, W.B.1    Shen, J.2    Gai, D.3    Chen, X.S.4
  • 8
    • 77952034643 scopus 로고    scopus 로고
    • Engineered interfaces of an AAA+ ATPase reveal a new nucleotide-dependent coordination mechanism
    • Joly N., Buck M. Engineered interfaces of an AAA+ ATPase reveal a new nucleotide-dependent coordination mechanism. J. Biol. Chem. 2010, 285:15178-15186.
    • (2010) J. Biol. Chem. , vol.285 , pp. 15178-15186
    • Joly, N.1    Buck, M.2
  • 9
    • 33845919591 scopus 로고    scopus 로고
    • Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activator
    • Joly N., Schumacher J., Buck M. Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activator. J. Biol. Chem. 2006, 281:34997-35007.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34997-35007
    • Joly, N.1    Schumacher, J.2    Buck, M.3
  • 10
    • 35448968986 scopus 로고    scopus 로고
    • Coupling nucleotide hydrolysis to transcription activation performance in a bacterial enhancer binding protein
    • Joly N., Rappas M., Wigneshweraraj S.R., Zhang X., Buck M. Coupling nucleotide hydrolysis to transcription activation performance in a bacterial enhancer binding protein. Mol. Microbiol. 2007, 66:583-595.
    • (2007) Mol. Microbiol. , vol.66 , pp. 583-595
    • Joly, N.1    Rappas, M.2    Wigneshweraraj, S.R.3    Zhang, X.4    Buck, M.5
  • 11
    • 46649108584 scopus 로고    scopus 로고
    • An intramolecular route for coupling ATPase activity in AAA+ proteins for transcription activation
    • Joly N., Burrows P.C., Buck M. An intramolecular route for coupling ATPase activity in AAA+ proteins for transcription activation. J. Biol. Chem. 2008, 283:13725-13735.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13725-13735
    • Joly, N.1    Burrows, P.C.2    Buck, M.3
  • 12
    • 77955127606 scopus 로고    scopus 로고
    • Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology
    • Joly N., Engl C., Jovanovic G., Huvet M., Toni T., Sheng X., Stumpf M.P., Buck M. Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. FEMS Microbiol. Rev. 2010, 34:797-827.
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 797-827
    • Joly, N.1    Engl, C.2    Jovanovic, G.3    Huvet, M.4    Toni, T.5    Sheng, X.6    Stumpf, M.P.7    Buck, M.8
  • 13
    • 84855207431 scopus 로고    scopus 로고
    • Coupling AAA protein function to regulated gene expression
    • Joly N., Zhang N., Buck M., Zhang X. Coupling AAA protein function to regulated gene expression. Biochim. Biophys. Acta 2012, 1823:108-116.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 108-116
    • Joly, N.1    Zhang, N.2    Buck, M.3    Zhang, X.4
  • 14
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 1998, 94:525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 15
    • 0033634866 scopus 로고    scopus 로고
    • Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control
    • Liu J., Smith C.L., DeRyckere D., DeAngelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell 2000, 6:637-648.
    • (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
  • 16
    • 35348971984 scopus 로고    scopus 로고
    • ATPase site architecture and helicase mechanism of an archaeal MCM
    • Moreau M.J., McGeoch A.T., Lowe A.R., Itzhaki L.S., Bell S.D. ATPase site architecture and helicase mechanism of an archaeal MCM. Mol. Cell 2007, 28:304-314.
    • (2007) Mol. Cell , vol.28 , pp. 304-314
    • Moreau, M.J.1    McGeoch, A.T.2    Lowe, A.R.3    Itzhaki, L.S.4    Bell, S.D.5
  • 17
    • 0023809599 scopus 로고
    • Coupled assay of Na+,K+-ATPase activity
    • Nørby J.G. Coupled assay of Na+,K+-ATPase activity. Methods Enzymol. 1988, 156:116-119.
    • (1988) Methods Enzymol. , vol.156 , pp. 116-119
    • Nørby, J.G.1
  • 18
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: common structure-diverse function
    • Ogura T., Wilkinson A.J. AAA+ superfamily ATPases: common structure-diverse function. Genes Cells 2001, 6:575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 19
    • 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 S.W., Wilkinson A.J. Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases. J. Struct. Biol. 2004, 146:106-112.
    • (2004) J. Struct. Biol. , vol.146 , pp. 106-112
    • Ogura, T.1    Whiteheart, S.W.2    Wilkinson, A.J.3
  • 21
    • 33344469160 scopus 로고    scopus 로고
    • Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF
    • Rappas M., Schumacher J., Niwa H., Buck M., Zhang X. Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF. J. Mol. Biol. 2006, 357:481-492.
    • (2006) J. Mol. Biol. , vol.357 , pp. 481-492
    • Rappas, M.1    Schumacher, J.2    Niwa, H.3    Buck, M.4    Zhang, X.5
  • 24
    • 2142707172 scopus 로고    scopus 로고
    • ATP-dependent transcriptional activation by bacterial PspF AAA+protein
    • Schumacher J., Zhang X., Jones S., Bordes P., Buck M. ATP-dependent transcriptional activation by bacterial PspF AAA+protein. J. Mol. Biol. 2004, 338:863-875.
    • (2004) J. Mol. Biol. , vol.338 , pp. 863-875
    • Schumacher, J.1    Zhang, X.2    Jones, S.3    Bordes, P.4    Buck, M.5
  • 26
    • 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 J.E., Saraste M., Runswick M.J., Gay N.J. 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. 1982, 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
  • 27
    • 84855198520 scopus 로고    scopus 로고
    • Structure and function of the AAA+ nucleotide binding pocket
    • Wendler P., Ciniawsky S., Kock M., Kube S. Structure and function of the AAA+ nucleotide binding pocket. Biochim. Biophys. Acta 2012, 1823:2-14.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 2-14
    • Wendler, P.1    Ciniawsky, S.2    Kock, M.3    Kube, S.4
  • 28
    • 0346750927 scopus 로고    scopus 로고
    • Enhancer-dependent transcription by bacterial RNA polymerase: the beta subunit downstream lobe is used by sigma 54 during open promoter complex formation
    • Wigneshweraraj S.R., Nechaev S., Bordes P., Jones S., Cannon W., Severinov K., Buck M. Enhancer-dependent transcription by bacterial RNA polymerase: the beta subunit downstream lobe is used by sigma 54 during open promoter complex formation. Methods Enzymol. 2003, 370:646-657.
    • (2003) Methods Enzymol. , vol.370 , pp. 646-657
    • Wigneshweraraj, S.R.1    Nechaev, S.2    Bordes, P.3    Jones, S.4    Cannon, W.5    Severinov, K.6    Buck, M.7
  • 29
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu R.C., Hanson P.I., Jahn R., Brünger A.T. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol. 1998, 5:803-811.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brünger, A.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.