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Volumn 383, Issue 2, 2008, Pages 380-389

Analysis of the Isolated SecA DEAD Motor Suggests a Mechanism for Chemical-Mechanical Coupling

Author keywords

ATP hydrolysis; DEAD motor; protein translocation; SecA; transition state

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; HELICASE; PROTEIN SECA;

EID: 52949097970     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.08.022     Document Type: Article
Times cited : (14)

References (42)
  • 1
    • 0026542763 scopus 로고
    • Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein
    • Koonin E.V., and Gorbalenya A.E. Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein. FEBS. Lett. 298 (1992) 6-8
    • (1992) FEBS. Lett. , vol.298 , pp. 6-8
    • Koonin, E.V.1    Gorbalenya, A.E.2
  • 3
    • 0035813158 scopus 로고    scopus 로고
    • Escherichia coli SecA helicase activity is not required in vivo for efficient protein translocation or autogenous regulation
    • Schmidt M.O., Brosh R.M., and Oliver D.B. Escherichia coli SecA helicase activity is not required in vivo for efficient protein translocation or autogenous regulation. J. Biol. Chem. 276 (2001) 37076-37085
    • (2001) J. Biol. Chem. , vol.276 , pp. 37076-37085
    • Schmidt, M.O.1    Brosh, R.M.2    Oliver, D.B.3
  • 4
    • 0025847517 scopus 로고
    • Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli
    • Kimura E., Akita M., Matsuyama S., and Mizushima S. Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli. J. Biol. Chem. 266 (1991) 6600-6606
    • (1991) J. Biol. Chem. , vol.266 , pp. 6600-6606
    • Kimura, E.1    Akita, M.2    Matsuyama, S.3    Mizushima, S.4
  • 5
    • 0033774991 scopus 로고    scopus 로고
    • Tyr-326 plays a critical role in controlling SecA-preprotein interaction
    • Kourtz L., and Oliver D. Tyr-326 plays a critical role in controlling SecA-preprotein interaction. Mol. Microbiol. 37 (2000) 1342-1356
    • (2000) Mol. Microbiol. , vol.37 , pp. 1342-1356
    • Kourtz, L.1    Oliver, D.2
  • 7
    • 36049046667 scopus 로고    scopus 로고
    • Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR
    • Gelis I., Bonvin A.M., Keramisanou D., Koukaki M., Gouridis G., Karamanou S., et al. Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR. Cell 131 (2007) 756-769
    • (2007) Cell , vol.131 , pp. 756-769
    • Gelis, I.1    Bonvin, A.M.2    Keramisanou, D.3    Koukaki, M.4    Gouridis, G.5    Karamanou, S.6
  • 8
    • 3343011973 scopus 로고    scopus 로고
    • A large conformational change of the translocation ATPase SecA
    • Osborne A.R., Clemons W.M., and Rapoport T.A. A large conformational change of the translocation ATPase SecA. Proc. Natl Acad. Sci. USA 101 (2004) 10937-10942
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10937-10942
    • Osborne, A.R.1    Clemons, W.M.2    Rapoport, T.A.3
  • 9
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • Hartl F., Lecker S., Schiebel E., Hendrick J., and Wickner W. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell 63 (1990) 269-279
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.4    Wickner, W.5
  • 10
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • Lill R., Dowhan W., and Wickner W. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell 60 (1990) 271-280
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 11
    • 0037144467 scopus 로고    scopus 로고
    • Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA
    • Hunt J.F., Weinkauf S., Henry L., Fak J.J., McNicholas P., Oliver D.B., and Deisenhofer J. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science 297 (2002) 2018-2226
    • (2002) Science , vol.297 , pp. 2018-2226
    • Hunt, J.F.1    Weinkauf, S.2    Henry, L.3    Fak, J.J.4    McNicholas, P.5    Oliver, D.B.6    Deisenhofer, J.7
  • 13
    • 33750846046 scopus 로고    scopus 로고
    • Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer
    • Vassylyev D.G., Mori H., Vassylyeva M.N., Tsukazaki T., Kimura Y., Tahirov T.H., and Ito K. Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer. J. Mol. Biol. 364 (2006) 248-258
    • (2006) J. Mol. Biol. , vol.364 , pp. 248-258
    • Vassylyev, D.G.1    Mori, H.2    Vassylyeva, M.N.3    Tsukazaki, T.4    Kimura, Y.5    Tahirov, T.H.6    Ito, K.7
  • 15
    • 0034637517 scopus 로고    scopus 로고
    • Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase
    • Dapic V., and Oliver D. Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase. J. Biol. Chem. 275 (2000) 22507-25000
    • (2000) J. Biol. Chem. , vol.275 , pp. 22507-25000
    • Dapic, V.1    Oliver, D.2
  • 16
    • 0035374515 scopus 로고    scopus 로고
    • Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity
    • Triplett T.L., Sgrignoli A.R., Gao F.B., Yang Y.B., Tai P.C., and Gierasch L.M. Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity. J. Biol. Chem. 276 (2001) 19648-19655
    • (2001) J. Biol. Chem. , vol.276 , pp. 19648-19655
    • Triplett, T.L.1    Sgrignoli, A.R.2    Gao, F.B.3    Yang, Y.B.4    Tai, P.C.5    Gierasch, L.M.6
  • 17
    • 0033428711 scopus 로고    scopus 로고
    • A molecular switch in SecA protein couples ATP hydrolysis to protein translocation
    • Karamanou S., Vrontou E., Sianidis G., Baud C., Roos T., Kuhn A., et al. A molecular switch in SecA protein couples ATP hydrolysis to protein translocation. Mol. Microbiol. 34 (1999) 1133-1145
    • (1999) Mol. Microbiol. , vol.34 , pp. 1133-1145
    • Karamanou, S.1    Vrontou, E.2    Sianidis, G.3    Baud, C.4    Roos, T.5    Kuhn, A.6
  • 18
    • 17644384428 scopus 로고    scopus 로고
    • Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism
    • Zito C.R., Antony E., Hunt J.F., Oliver D.B., and Hingorani M.M. Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism. J. Biol. Chem. 280 (2005) 14611-14619
    • (2005) J. Biol. Chem. , vol.280 , pp. 14611-14619
    • Zito, C.R.1    Antony, E.2    Hunt, J.F.3    Oliver, D.B.4    Hingorani, M.M.5
  • 21
    • 0027488666 scopus 로고
    • Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase
    • Mitchell C., and Oliver D. Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase. Mol. Microbiol. 10 (1993) 483-497
    • (1993) Mol. Microbiol. , vol.10 , pp. 483-497
    • Mitchell, C.1    Oliver, D.2
  • 22
    • 0029811785 scopus 로고    scopus 로고
    • Domain interactions of the peripheral preprotein translocase subunit SecA
    • den Blaauwen T., Fekkes P., de Wit J.G., Kuiper W., and Driessen A.J. Domain interactions of the peripheral preprotein translocase subunit SecA. Biochemistry 35 (1996) 11994-12004
    • (1996) Biochemistry , vol.35 , pp. 11994-12004
    • den Blaauwen, T.1    Fekkes, P.2    de Wit, J.G.3    Kuiper, W.4    Driessen, A.J.5
  • 23
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O., Banroques J., Tanner N.K., and Linder P. The DEAD-box protein family of RNA helicases. Gene 367 (2006) 17-37
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 24
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku T., Nureki O., Nakamura A., Kobayashi S., and Yokoyama S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 125 (2006) 287-300
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 25
    • 0037252143 scopus 로고    scopus 로고
    • The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis
    • Tanner N.K., Cordin O., Banroques J., Doère M., and Linder P. The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis. Mol. Cell. 11 (2003) 127-138
    • (2003) Mol. Cell. , vol.11 , pp. 127-138
    • Tanner, N.K.1    Cordin, O.2    Banroques, J.3    Doère, M.4    Linder, P.5
  • 26
    • 4444316122 scopus 로고    scopus 로고
    • Helicase Motif III in SecA is essential for coupling preprotein binding to translocation ATPase
    • Papanikou E., Karamanou S., Baud C., Sianidis G., Frank M., and Economou A. Helicase Motif III in SecA is essential for coupling preprotein binding to translocation ATPase. EMBO Rep. 5 (2004) 807-811
    • (2004) EMBO Rep. , vol.5 , pp. 807-811
    • Papanikou, E.1    Karamanou, S.2    Baud, C.3    Sianidis, G.4    Frank, M.5    Economou, A.6
  • 27
    • 0035282958 scopus 로고    scopus 로고
    • Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function
    • Sianidis G., Karamanou S., Vrontou E., Boulias K., Repanas K., Kyrpides N., et al. Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function. EMBO J. 20 (2001) 961-970
    • (2001) EMBO J. , vol.20 , pp. 961-970
    • Sianidis, G.1    Karamanou, S.2    Vrontou, E.3    Boulias, K.4    Repanas, K.5    Kyrpides, N.6
  • 29
    • 3042640723 scopus 로고    scopus 로고
    • Rotation of F1-ATPase: how an ATP-driven molecular machine may work
    • Kinosita K., Adachi K., and Itoh H. Rotation of F1-ATPase: how an ATP-driven molecular machine may work. Annu. Rev. Biophys. Biomol. Struct. 33 (2004) 245-268
    • (2004) Annu. Rev. Biophys. Biomol. Struct. , vol.33 , pp. 245-268
    • Kinosita, K.1    Adachi, K.2    Itoh, H.3
  • 30
    • 33744806329 scopus 로고    scopus 로고
    • Simple models for extracting mechanical work from the ATP hydrolysis cycle
    • Eide J.L., Chakraborty A.K., and Oster G.F. Simple models for extracting mechanical work from the ATP hydrolysis cycle. Biophys. J. 90 (2006) 4281-4294
    • (2006) Biophys. J. , vol.90 , pp. 4281-4294
    • Eide, J.L.1    Chakraborty, A.K.2    Oster, G.F.3
  • 31
    • 0025840280 scopus 로고
    • The first gene in the Escherichia coli SecA operon, gene X, encodes a nonessential secretory protein
    • Rajapandi T., Dolan K.M., and Oliver D.B. The first gene in the Escherichia coli SecA operon, gene X, encodes a nonessential secretory protein. J. Bacteriol. 173 (1991) 7092-7097
    • (1991) J. Bacteriol. , vol.173 , pp. 7092-7097
    • Rajapandi, T.1    Dolan, K.M.2    Oliver, D.B.3
  • 32
    • 0036303451 scopus 로고    scopus 로고
    • The ATPase domain of SecA can form a tetramer in solution
    • Dempsey B.R., Economou A., Dunn S.D., and Shilton B.H. The ATPase domain of SecA can form a tetramer in solution. J. Mol. Biol. 315 (2002) 831-843
    • (2002) J. Mol. Biol. , vol.315 , pp. 831-843
    • Dempsey, B.R.1    Economou, A.2    Dunn, S.D.3    Shilton, B.H.4
  • 33
    • 0031106816 scopus 로고    scopus 로고
    • A continuous spectrophotometric assay for aspartate transcarbamylase and ATPases
    • Rieger C.E., Lee J., and Turnbull J.L. A continuous spectrophotometric assay for aspartate transcarbamylase and ATPases. Anal. Biochem. 246 (1997) 86-95
    • (1997) Anal. Biochem. , vol.246 , pp. 86-95
    • Rieger, C.E.1    Lee, J.2    Turnbull, J.L.3
  • 34
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Williston S., Brandts J.F., and Lin L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179 (1989) 131-137
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 37
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 38
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 40
    • 0026597444 scopus 로고
    • Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.1
  • 42
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.2    Moss, D.S.3    Thornton, J.M.4


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