메뉴 건너뛰기




Volumn 14, Issue 12, 2009, Pages 1405-1413

Temperature-dependent regulation of Thermus thermophilus DnaK/DnaJ chaperones by DafA protein

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN DAFA; PROTEIN DNAJ; PROTEIN DNAK; UNCLASSIFIED DRUG;

EID: 71649106232     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/j.1365-2443.2009.01357.x     Document Type: Article
Times cited : (8)

References (28)
  • 1
    • 33845922099 scopus 로고    scopus 로고
    • Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein
    • Bird JG, Sharma S, Roshwalb SC, Hoskins JR, Wickner S. Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein. J. Biol. Chem. 2006, 281:34349-34356.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34349-34356
    • Bird, J.G.1    Sharma, S.2    Roshwalb, S.C.3    Hoskins, J.R.4    Wickner, S.5
  • 2
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 3
    • 4043103993 scopus 로고    scopus 로고
    • CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM
    • Chae C, Sharma S, Hoskins JR, Wickner S. CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM. J. Biol. Chem. 2004, 279:33147-33153.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33147-33153
    • Chae, C.1    Sharma, S.2    Hoskins, J.R.3    Wickner, S.4
  • 4
    • 34247632202 scopus 로고    scopus 로고
    • In vivo modulation of a DnaJ homolog, CbpA, by CbpM
    • Chenoweth MR, Trun N, Wickner S. In vivo modulation of a DnaJ homolog, CbpA, by CbpM. J. Bacteriol. 2007, 189:3635-3638.
    • (2007) J. Bacteriol. , vol.189 , pp. 3635-3638
    • Chenoweth, M.R.1    Trun, N.2    Wickner, S.3
  • 5
    • 48149104997 scopus 로고    scopus 로고
    • Complex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM
    • Chenoweth MR, Wickner S. Complex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM. J. Bacteriol. 2008, 190:5153-5161.
    • (2008) J. Bacteriol. , vol.190 , pp. 5153-5161
    • Chenoweth, M.R.1    Wickner, S.2
  • 6
    • 0034647887 scopus 로고    scopus 로고
    • Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
    • Diamant S, Ben-Zvi AP, Bukau B, Goloubinoff P. Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J. Biol. Chem. 2000, 275:21107-21113.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21107-21113
    • Diamant, S.1    Ben-Zvi, A.P.2    Bukau, B.3    Goloubinoff, P.4
  • 8
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    • Glover JR, Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 1998, 94:73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 9
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl Acad. Sci. USA 1999, 96:13732-13737.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 10
    • 0037805634 scopus 로고    scopus 로고
    • Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures
    • Grimshaw JP, Jelesarov I, Siegenthaler RK, Christen P. Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures. J. Biol. Chem. 2003, 278:19048-19053.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19048-19053
    • Grimshaw, J.P.1    Jelesarov, I.2    Siegenthaler, R.K.3    Christen, P.4
  • 11
    • 0035793209 scopus 로고    scopus 로고
    • Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE
    • Groemping Y, Klostermeier D, Herrmann C, Veit T, Seidel R, Reinstein J. Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE. J. Mol. Biol. 2001, 305:1173-1183.
    • (2001) J. Mol. Biol. , vol.305 , pp. 1173-1183
    • Groemping, Y.1    Klostermeier, D.2    Herrmann, C.3    Veit, T.4    Seidel, R.5    Reinstein, J.6
  • 12
    • 0035900534 scopus 로고    scopus 로고
    • Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response
    • Groemping Y, Reinstein J. Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response. J. Mol. Biol. 2001, 314:167-178.
    • (2001) J. Mol. Biol. , vol.314 , pp. 167-178
    • Groemping, Y.1    Reinstein, J.2
  • 13
    • 0033515528 scopus 로고    scopus 로고
    • The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system
    • Klostermeier D, Seidel R, Reinstein J. The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. J. Mol. Biol. 1999, 287:511-525.
    • (1999) J. Mol. Biol. , vol.287 , pp. 511-525
    • Klostermeier, D.1    Seidel, R.2    Reinstein, J.3
  • 14
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • Mogk A, Schlieker C, Friedrich KL, Schonfeld HJ, Vierling E, Bukau B. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J. Biol. Chem. 2003, 278:31033-31042.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31033-31042
    • Mogk, A.1    Schlieker, C.2    Friedrich, K.L.3    Schonfeld, H.J.4    Vierling, E.5    Bukau, B.6
  • 15
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB
    • Mogk A, Tomoyasu T, Goloubinoff P, Rudiger S, Roder D, Langen H, Bukau B. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 1999, 18:6934-6949.
    • (1999) EMBO J. , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6    Bukau, B.7
  • 16
    • 0027984270 scopus 로고
    • Isolation of the stable hexameric DnaK.DnaJ complex from Thermus thermophilus
    • Motohashi K, Taguchi H, Ishii N, Yoshida M. Isolation of the stable hexameric DnaK.DnaJ complex from Thermus thermophilus. J. Biol. Chem. 1994, 269:27074-27079.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27074-27079
    • Motohashi, K.1    Taguchi, H.2    Ishii, N.3    Yoshida, M.4
  • 17
    • 0030054723 scopus 로고    scopus 로고
    • A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus
    • Motohashi K, Yohda M, Endo I, Yoshida M. A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus. J. Biol. Chem. 1996, 271:17343-17348.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17343-17348
    • Motohashi, K.1    Yohda, M.2    Endo, I.3    Yoshida, M.4
  • 18
    • 0030832411 scopus 로고    scopus 로고
    • K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of DnaK x DnaJ complex from Thermus thermophilus
    • Motohashi K, Yohda M, Odaka M, Yoshida M. K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of DnaK x DnaJ complex from Thermus thermophilus. FEBS Lett. 1997, 412:633-636.
    • (1997) FEBS Lett. , vol.412 , pp. 633-636
    • Motohashi, K.1    Yohda, M.2    Odaka, M.3    Yoshida, M.4
  • 19
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones
    • Motohashi K, Watanabe Y, Yohda M, Yoshida M. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc. Natl Acad. Sci. USA 1999, 96:7184-7189.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 20
    • 0022349286 scopus 로고
    • Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus
    • Okuno H, Nagata K, Nakajima H. Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus. J. Appl. Biochem. 1985, 7:192-201.
    • (1985) J. Appl. Biochem. , vol.7 , pp. 192-201
    • Okuno, H.1    Nagata, K.2    Nakajima, H.3
  • 21
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 1987, 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 22
    • 0035793721 scopus 로고    scopus 로고
    • The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites
    • Schlee S, Groemping Y, Herde P, Seidel R, Reinstein J. The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites. J. Mol. Biol. 2001, 306:889-899.
    • (2001) J. Mol. Biol. , vol.306 , pp. 889-899
    • Schlee, S.1    Groemping, Y.2    Herde, P.3    Seidel, R.4    Reinstein, J.5
  • 23
    • 17644407779 scopus 로고    scopus 로고
    • The importance of having thermosensor control in the DnaK chaperone system
    • Siegenthaler RK, Christen P. The importance of having thermosensor control in the DnaK chaperone system. J. Biol. Chem. 2005, 280:14395-14401.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14395-14401
    • Siegenthaler, R.K.1    Christen, P.2
  • 24
    • 21644468868 scopus 로고    scopus 로고
    • ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2
    • Watanabe YH, Takano M, Yoshida M. ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2. J. Biol. Chem. 2005, 280:24562-24567.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24562-24567
    • Watanabe, Y.H.1    Takano, M.2    Yoshida, M.3
  • 25
    • 1942501822 scopus 로고    scopus 로고
    • Trigonal DnaK-DnaJ complex versus free DnaK and DnaJ: heat stress converts the former to the latter, and only the latter can do disaggregation in cooperation with ClpB
    • Watanabe YH, Yoshida M. Trigonal DnaK-DnaJ complex versus free DnaK and DnaJ: heat stress converts the former to the latter, and only the latter can do disaggregation in cooperation with ClpB. J. Biol. Chem. 2004, 279:15723-15727.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15723-15727
    • Watanabe, Y.H.1    Yoshida, M.2
  • 26
    • 0034724719 scopus 로고    scopus 로고
    • Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form
    • Watanabe YH, Motohashi K, Taguchi H, Yoshida M. Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form. J. Biol. Chem. 2000, 275:12388-12392.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12388-12392
    • Watanabe, Y.H.1    Motohashi, K.2    Taguchi, H.3    Yoshida, M.4
  • 27
    • 0037155139 scopus 로고    scopus 로고
    • Roles of the two ATP binding sites of ClpB from Thermus thermophilus
    • Watanabe YH, Motohashi K, Yoshida M. Roles of the two ATP binding sites of ClpB from Thermus thermophilus. J. Biol. Chem. 2002, 277:5804-5809.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5804-5809
    • Watanabe, Y.H.1    Motohashi, K.2    Yoshida, M.3
  • 28
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
    • Zolkiewski M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J. Biol. Chem. 1999, 274:28083-28086.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.