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Volumn 289, Issue 44, 2014, Pages 30343-30354

Zinc and ATP binding of the hexameric AAA-ATPase PilF from Thermus thermophilus: Role in complex stability, piliation, adhesion, twitching motility, and natural transformation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; COORDINATION REACTIONS; STABILITY;

EID: 84910030858     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.598656     Document Type: Article
Times cited : (23)

References (42)
  • 1
    • 0028136885 scopus 로고
    • Bacterial gene transfer by natural genetic transformation in the environment
    • Lorenz, M. G., and Wackernagel, W. (1994) Bacterial gene transfer by natural genetic transformation in the environment. Microbiol. Rev. 58, 563-602
    • (1994) Microbiol. Rev. , vol.58 , pp. 563-602
    • Lorenz, M.G.1    Wackernagel, W.2
  • 2
    • 64349085688 scopus 로고    scopus 로고
    • The natural transformation system of Acinetobacter baylyi ADP1: A unique DNA transport machinery
    • Gerischer, U., ed., Caister Academic Press, Norfolk, UK
    • Averhoff, B., and Graf, I. (2008) The natural transformation system of Acinetobacter baylyi ADP1: a unique DNA transport machinery. In Acinetobacter Molecular Biology (Gerischer, U., ed.) pp. 119-140, Caister Academic Press, Norfolk, UK
    • (2008) Acinetobacter Molecular Biology , pp. 119-140
    • Averhoff, B.1    Graf, I.2
  • 3
    • 0032697140 scopus 로고    scopus 로고
    • DNA uptake in bacteria
    • Dubnau, D. (1999) DNA uptake in bacteria. Annu. Rev. Microbiol. 53, 217-244
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 217-244
    • Dubnau, D.1
  • 4
    • 64349100581 scopus 로고    scopus 로고
    • Shuffling genes around in hot environments: The unique DNA transporter of Thermus thermophilus
    • Averhoff, B. (2009) Shuffling genes around in hot environments: the unique DNA transporter of Thermus thermophilus. FEMS Microbiol. Rev. 33, 611-626
    • (2009) FEMS Microbiol. Rev. , vol.33 , pp. 611-626
    • Averhoff, B.1
  • 5
    • 0022448655 scopus 로고
    • Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp
    • Koyama, Y., Hoshino, T., Tomizuka, N, and Furukawa, K. (1986) Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp. J. Bacteriol. 166, 338-340
    • (1986) J. Bacteriol. , vol.166 , pp. 338-340
    • Koyama, Y.1    Hoshino, T.2    Tomizuka, N.3    Furukawa, K.4
  • 6
    • 79953227678 scopus 로고    scopus 로고
    • Structure and function of PilQ, a secretin of the DNA transporter from the thermophilic bacterium Thermus thermophilus HB27
    • Burkhardt, J., Vonck, J., and Averhoff, B. (2011) Structure and function of PilQ, a secretin of the DNA transporter from the thermophilic bacterium Thermus thermophilus HB27. J. Biol. Chem. 286, 9977-9984
    • (2011) J. Biol. Chem. , vol.286 , pp. 9977-9984
    • Burkhardt, J.1    Vonck, J.2    Averhoff, B.3
  • 7
    • 84858054413 scopus 로고    scopus 로고
    • Unusual N-terminal aafiafifia fold of PilQ from Thermus thermophilus mediates ring formation and is essential for piliation
    • Burkhardt, J., Vonck, J., Langer, J. D., Salzer, R., and Averhoff, B. (2012) Unusual N-terminal aafiafifia fold of PilQ from Thermus thermophilus mediates ring formation and is essential for piliation. J. Biol. Chem. 287, 8484-8494
    • (2012) J. Biol. Chem. , vol.287 , pp. 8484-8494
    • Burkhardt, J.1    Vonck, J.2    Langer, J.D.3    Salzer, R.4    Averhoff, B.5
  • 8
    • 0036151806 scopus 로고    scopus 로고
    • Molecular analyses of the natural transformation machinery and identification of pilus structures in the extremely thermophilic bacterium Thermus thermophilus strain HB27
    • Friedrich, A., Prust, C., Hartsch, T., Henne, A., and Averhoff, B. (2002) Molecular analyses of the natural transformation machinery and identification of pilus structures in the extremely thermophilic bacterium Thermus thermophilus strain HB27. Appl. Environ. Microbiol. 68, 745-755
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 745-755
    • Friedrich, A.1    Prust, C.2    Hartsch, T.3    Henne, A.4    Averhoff, B.5
  • 9
    • 33748317821 scopus 로고    scopus 로고
    • Characterization of DNA transport in the thermophilic bacterium Thermus thermophilus HB27
    • Schwarzenlander, C., and Averhoff, B. (2006) Characterization of DNA transport in the thermophilic bacterium Thermus thermophilus HB27. FEBS J. 273, 4210-4218
    • (2006) FEBS J. , vol.273 , pp. 4210-4218
    • Schwarzenlander, C.1    Averhoff, B.2
  • 10
    • 0037817408 scopus 로고    scopus 로고
    • Pilin-like proteins in the extremely thermophilic bacterium Thermus thermophilus HB27: Implication in competence for natural transformation and links to type IV pilus biogenesis
    • Friedrich, A., Rumszauer, J., Henne, A., and Averhoff, B. (2003) Pilin-like proteins in the extremely thermophilic bacterium Thermus thermophilus HB27: implication in competence for natural transformation and links to type IV pilus biogenesis. Appl. Environ. Microbiol. 69, 3695-3700
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3695-3700
    • Friedrich, A.1    Rumszauer, J.2    Henne, A.3    Averhoff, B.4
  • 11
    • 63849107738 scopus 로고    scopus 로고
    • The role of single subunits of the DNA transport machinery of Thermus thermophilus HB27 in DNA binding and transport
    • Schwarzenlander, C., Haase, W., and Averhoff, B. (2009) The role of single subunits of the DNA transport machinery of Thermus thermophilus HB27 in DNA binding and transport. Environ. Microbiol. 11, 801-808
    • (2009) Environ. Microbiol. , vol.11 , pp. 801-808
    • Schwarzenlander, C.1    Haase, W.2    Averhoff, B.3
  • 12
    • 33745614951 scopus 로고    scopus 로고
    • Identification, subcellular localization, and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27
    • Rumszauer, J., Schwarzenlander, C., and Averhoff, B. (2006) Identification, subcellular localization, and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27. FEBS J. 273, 3261-3272
    • (2006) FEBS J. , vol.273 , pp. 3261-3272
    • Rumszauer, J.1    Schwarzenlander, C.2    Averhoff, B.3
  • 13
    • 84892462311 scopus 로고    scopus 로고
    • Type IV pilus biogenesis, twitching motility, and DNA uptake in Thermus thermophilus: Discrete roles of antagonistic ATPases PilF, PilT1, and PilT2
    • Salzer, R., Joos, F., and Averhoff, B. (2014) Type IV pilus biogenesis, twitching motility, and DNA uptake in Thermus thermophilus: discrete roles of antagonistic ATPases PilF, PilT1, and PilT2. Appl. Environ. Microbiol. 80, 644-652
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 644-652
    • Salzer, R.1    Joos, F.2    Averhoff, B.3
  • 14
    • 79952245317 scopus 로고    scopus 로고
    • Identification and characterization of a unique, zinc-containing transport ATPase essential for natural transformation in Thermus thermophilus HB27
    • Rose, I., Biukovic, G., Aderhold, P., Müller, V., Grüber, G., and Averhoff, B. (2011) Identification and characterization of a unique, zinc-containing transport ATPase essential for natural transformation in Thermus thermophilus HB27. Extremophiles 15, 191-202
    • (2011) Extremophiles , vol.15 , pp. 191-202
    • Rose, I.1    Biukovic, G.2    Aderhold, P.3    Müller, V.4    Grüber, G.5    Averhoff, B.6
  • 15
    • 84874074962 scopus 로고    scopus 로고
    • Structure and mechanism of the PilF DNA transformation ATPase from Thermus thermophilus
    • Collins, R. F., Hassan, D., Karuppiah, V., Thistlethwaite, A., and Derrick, J. P. (2013) Structure and mechanism of the PilF DNA transformation ATPase from Thermus thermophilus. Biochem. J. 450, 417-425
    • (2013) Biochem. J. , vol.450 , pp. 417-425
    • Collins, R.F.1    Hassan, D.2    Karuppiah, V.3    Thistlethwaite, A.4    Derrick, J.P.5
  • 16
    • 84873799110 scopus 로고
    • Studies on lysogenesis
    • Bertani, G. (1951) Studies on lysogenesis. J. Bacteriol. 62, 293-300
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1
  • 17
    • 85008065603 scopus 로고
    • Isolation of an extreme thermophile and thermostability of its transfer ribonucleic acid and ribosomes
    • Oshima, T., and Imahori, K. (1971) Isolation of an extreme thermophile and thermostability of its transfer ribonucleic acid and ribosomes. J. Gen. Appl. Microbiol. 17, 513-517
    • (1971) J. Gen. Appl. Microbiol. , vol.17 , pp. 513-517
    • Oshima, T.1    Imahori, K.2
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 28444497467 scopus 로고    scopus 로고
    • Advantages and limitations of clearnative PAGE
    • Wittig, I., and Schägger, H. (2005) Advantages and limitations of clearnative PAGE. Proteomics 5, 4338-4346
    • (2005) Proteomics , vol.5 , pp. 4338-4346
    • Wittig, I.1    Schägger, H.2
  • 21
    • 0019830545 scopus 로고
    • A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase
    • Heinonen, J. K., and Lahti, R. J. (1981) A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase. Anal. Biochem. 113, 313-317
    • (1981) Anal. Biochem. , vol.113 , pp. 313-317
    • Heinonen, J.K.1    Lahti, R.J.2
  • 22
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen, F. H., Berglund, H., and Vedadi, M. (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2, 2212-2221
    • (2007) Nat. Protoc. , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 23
    • 84905564500 scopus 로고    scopus 로고
    • Environmental factors affecting the expression of type IV pilus genes as well as piliation of Thermus thermophilus
    • Salzer, R., Kern, T., Joos, F., and Averhoff, B. (2014) Environmental factors affecting the expression of type IV pilus genes as well as piliation of Thermus thermophilus. FEMS Microbiol. Lett. 357, 56-62
    • (2014) FEMS Microbiol. Lett. , vol.357 , pp. 56-62
    • Salzer, R.1    Kern, T.2    Joos, F.3    Averhoff, B.4
  • 24
    • 0035408426 scopus 로고    scopus 로고
    • Natural transformation in mesophilic and thermophilic bacteria: Identification and characterization of novel, closely related competence genes in Acinetobacter sp. Strain BD413 and Thermus thermophilus HB27
    • Friedrich, A., Hartsch, T., and Averhoff, B. (2001) Natural transformation in mesophilic and thermophilic bacteria: identification and characterization of novel, closely related competence genes in Acinetobacter sp. strain BD413 and Thermus thermophilus HB27. Appl. Environ. Microbiol. 67, 3140-3148
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3140-3148
    • Friedrich, A.1    Hartsch, T.2    Averhoff, B.3
  • 25
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee, B. L., and Auld, D. S. (1990) Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29, 5647-5659
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 26
    • 0242360953 scopus 로고    scopus 로고
    • DNA transport during transformation
    • Chen, I., and Dubnau, D. (2003) DNA transport during transformation. Front. Biosci. 8, 544-556
    • (2003) Front. Biosci. , vol.8 , pp. 544-556
    • Chen, I.1    Dubnau, D.2
  • 27
    • 0027489247 scopus 로고
    • Common componentsinthe assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and proteinsecretion apparatus: A general system for the formation of surface-associated protein complexes
    • Hobbs, M., and Mattick, J. S. (1993) Common componentsinthe assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and proteinsecretion apparatus: a general system for the formation of surface-associated protein complexes. Mol. Microbiol. 10, 233-243
    • (1993) Mol. Microbiol. , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 28
    • 0033214349 scopus 로고    scopus 로고
    • Bacterial typeIIprotein export and pilus biogenesis: More than just homologies?
    • Nunn, D. (1999) Bacterial typeIIprotein export and pilus biogenesis: more than just homologies? Trends Cell Biol. 9, 402-408
    • (1999) Trends Cell Biol. , vol.9 , pp. 402-408
    • Nunn, D.1
  • 29
    • 0345306190 scopus 로고    scopus 로고
    • Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella
    • Peabody, C. R., Chung, Y. J., Yen, M. R., Vidal-Ingigliardi, D., Pugsley, A. P., and Saier, M. H., Jr. (2003) Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. Microbiology 149, 3051-3072
    • (2003) Microbiology , vol.149 , pp. 3051-3072
    • Peabody, C.R.1    Chung, Y.J.2    Yen, M.R.3    Vidal-Ingigliardi, D.4    Pugsley, A.P.5    Saier, M.H.6
  • 30
    • 0141862137 scopus 로고    scopus 로고
    • Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae
    • Robien, M. A., Krumm, B. E., Sandkvist, M., and Hol, W. G. (2003) Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae. J. Mol. Biol. 333, 657-674
    • (2003) J. Mol. Biol. , vol.333 , pp. 657-674
    • Robien, M.A.1    Krumm, B.E.2    Sandkvist, M.3    Hol, W.G.4
  • 31
    • 41549119041 scopus 로고    scopus 로고
    • PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus
    • Jakovljevic, V., Leonardy, S., Hoppert, M., and Søgaard-Andersen, L. (2008) PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus. J. Bacteriol. 190, 2411-2421
    • (2008) J. Bacteriol. , vol.190 , pp. 2411-2421
    • Jakovljevic, V.1    Leonardy, S.2    Hoppert, M.3    Søgaard-Andersen, L.4
  • 32
    • 11144271157 scopus 로고    scopus 로고
    • Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE
    • Camberg, J. L., and Sandkvist, M. (2005) Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE. J. Bacteriol. 187, 249-256
    • (2005) J. Bacteriol. , vol.187 , pp. 249-256
    • Camberg, J.L.1    Sandkvist, M.2
  • 34
    • 0034724415 scopus 로고    scopus 로고
    • Sequence-related protein export NTPases encoded by the conjugative transfer region of RP4 and by the cag pathogenicity island of Helicobacter pylori share similar hexameric ring structures
    • Krause, S., Barcena, M., Pansegrau, W., Lurz, R., Carazo, J. M., and Lanka, E. (2000) Sequence-related protein export NTPases encoded by the conjugative transfer region of RP4 and by the cag pathogenicity island of Helicobacter pylori share similar hexameric ring structures. Proc. Natl. Acad. Sci. U. S. A. 97, 3067-3072
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3067-3072
    • Krause, S.1    Barcena, M.2    Pansegrau, W.3    Lurz, R.4    Carazo, J.M.5    Lanka, E.6
  • 35
    • 33645734928 scopus 로고    scopus 로고
    • XpsE oligomerization triggered by ATP binding, not hydrolysis, leads to its association with XpsL
    • Shiue, S. J., Kao, K. M., Leu, W. M., Chen, L. Y., Chan, N. L., and Hu, N. T. (2006) XpsE oligomerization triggered by ATP binding, not hydrolysis, leads to its association with XpsL. EMBO J. 25, 1426-1435
    • (2006) EMBO J. , vol.25 , pp. 1426-1435
    • Shiue, S.J.1    Kao, K.M.2    Leu, W.M.3    Chen, L.Y.4    Chan, N.L.5    Hu, N.T.6
  • 37
    • 84896704461 scopus 로고    scopus 로고
    • ComEA is essential for the transfer of external DNA into the periplasm in naturally transformable Vibrio cholerae cells
    • Seitz, P., Pezeshgi Modarres, H., Borgeaud, S., Bulushev, R. D., Steinbock, L. J., Radenovic, A., Dal Peraro, M., and Blokesch, M. (2014) ComEA is essential for the transfer of external DNA into the periplasm in naturally transformable Vibrio cholerae cells. PLoS Genet. 10, e1004066
    • (2014) PLoS Genet. , vol.10 , pp. e1004066
    • Seitz, P.1    Modarres, P.H.2    Borgeaud, S.3    Bulushev, R.D.4    Steinbock, L.J.5    Radenovic, A.6    Dal Peraro, M.7    Blokesch, M.8
  • 39
    • 84898069901 scopus 로고    scopus 로고
    • Regulation of bacterial cell polarity by small GTPases
    • Keilberg, D., and Søgaard-Andersen, L. (2014) Regulation of bacterial cell polarity by small GTPases. Biochemistry 53, 1899-1907
    • (2014) Biochemistry , vol.53 , pp. 1899-1907
    • Keilberg, D.1    Søgaard-Andersen, L.2
  • 40
    • 84887087816 scopus 로고    scopus 로고
    • DNA-uptake machinery of naturally competentVibrio cholerae. Proc
    • Seitz, P., and Blokesch, M. (2013) DNA-uptake machinery of naturally competentVibrio cholerae. Proc. Natl. Acad. Sci. U. S. A. 110, 17987-17992
    • (2013) Natl. Acad. Sci. U. S. A. , vol.110 , pp. 17987-17992
    • Seitz, P.1    Blokesch, M.2
  • 42
    • 0015955554 scopus 로고
    • Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., A nonsporulating thermophilic bacterium from a Japanese thermal spa
    • Oshima, T., and Imahori, K. (1974) Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a nonsporulating thermophilic bacterium from a Japanese thermal spa. Int. J. Syst. Bacteriol. 24, 102-112
    • (1974) Int. J. Syst. Bacteriol. , vol.24 , pp. 102-112
    • Oshima, T.1    Imahori, K.2


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