메뉴 건너뛰기




Volumn 43, Issue 1, 2005, Pages 13-18

Co-immunoprecipitation of Hsp101 with cytosolic Hsc70

Author keywords

Complex; Hsc70; Hsp101; Hsp70; Immunoprecipitation; Maize

Indexed keywords

ANIMALIA; ARABIDOPSIS; ZEA MAYS;

EID: 14744292998     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2004.10.006     Document Type: Article
Times cited : (21)

References (38)
  • 1
    • 0037342584 scopus 로고    scopus 로고
    • Molecular characterization of rice Hsp101: Complementation of yeast Hsp104 mutation by disaggregation of protein granules and differential expression in indica and japonica rice types
    • M. Agarwal, C. Sahi, S. Katiyar-Agarwal, S. Agarwal, T. Young, D.R. Gallie, V.M. Sharma, K. Ganesan, and A. Grover Molecular characterization of rice Hsp101: complementation of yeast Hsp104 mutation by disaggregation of protein granules and differential expression in indica and japonica rice types Plant Mol. Biol 51 2003 543 553
    • (2003) Plant Mol. Biol , vol.51 , pp. 543-553
    • Agarwal, M.1    Sahi, C.2    Katiyar-Agarwal, S.3    Agarwal, S.4    Young, T.5    Gallie, D.R.6    Sharma, V.M.7    Ganesan, K.8    Grover, A.9
  • 2
    • 0028409108 scopus 로고
    • Differential influence of ATP on native spinach 70-kDa heat-shock cognates
    • J.V. Anderson, D.W. Haskell, and C.L. Guy Differential influence of ATP on native spinach 70-kDa heat-shock cognates Plant Physiol. 104 1994 1371 1380
    • (1994) Plant Physiol. , vol.104 , pp. 1371-1380
    • Anderson, J.V.1    Haskell, D.W.2    Guy, C.L.3
  • 3
    • 0028410560 scopus 로고
    • Structural organization of the spinach endoplasmic reticulum-luminal 70-kDa heat-shock cognate gene and expression of 70-kDa heat-shock genes during cold acclimation
    • J.V. Anderson, Q.B. Li, D.W. Haskell, and C.L. Guy Structural organization of the spinach endoplasmic reticulum-luminal 70-kDa heat-shock cognate gene and expression of 70-kDa heat-shock genes during cold acclimation Plant Physiol. 104 1994 1359 1370
    • (1994) Plant Physiol. , vol.104 , pp. 1359-1370
    • Anderson, J.V.1    Li, Q.B.2    Haskell, D.W.3    Guy, C.L.4
  • 4
    • 0031895122 scopus 로고    scopus 로고
    • Hsp90-containing multiprotein complexes in the eukaryotic microbe Achlya
    • S.A. Brunt, G.H. Perdew, D.O. Toft, and J.C. Silver Hsp90-containing multiprotein complexes in the eukaryotic microbe Achlya Cell Stress Chaperon 3 1998 44 56
    • (1998) Cell Stress Chaperon , vol.3 , pp. 44-56
    • Brunt, S.A.1    Perdew, G.H.2    Toft, D.O.3    Silver, J.C.4
  • 5
    • 0027985148 scopus 로고
    • Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae
    • H.C. Chang, and S. Lindquist Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae J. Biol. Chem. 269 1994 24983 24988
    • (1994) J. Biol. Chem. , vol.269 , pp. 24983-24988
    • Chang, H.C.1    Lindquist, S.2
  • 6
    • 0030834253 scopus 로고    scopus 로고
    • Heat shock protein 80 of Neurospora crassa, a cytosolic molecular chaperone of the eukaryotic stress 90 family, interacts directly with heat shock protein 70
    • D.G. Freitag, P.M. Ouimet, T.L. Girvitz, and M. Kapoor Heat shock protein 80 of Neurospora crassa, a cytosolic molecular chaperone of the eukaryotic stress 90 family, interacts directly with heat shock protein 70 Biochemistry 36 1997 10221 10229
    • (1997) Biochemistry , vol.36 , pp. 10221-10229
    • Freitag, D.G.1    Ouimet, P.M.2    Girvitz, T.L.3    Kapoor, M.4
  • 7
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • P. Goloubinoff, A. Mogk, A.P.B. Zvi, T. Tomoyasu, and B. Bukau Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network Proc. Natl. Acad. Sci. USA 96 1999 13732 13737
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.B.3    Tomoyasu, T.4    Bukau, B.5
  • 8
    • 0001594812 scopus 로고
    • Induction of freezing tolerance in spinach is associated with the synthesis of cold acclimation induced proteins
    • C.L. Guy, and D.W. Haskell Induction of freezing tolerance in spinach is associated with the synthesis of cold acclimation induced proteins Plant Physiol. 84 1987 872 878
    • (1987) Plant Physiol. , vol.84 , pp. 872-878
    • Guy, C.L.1    Haskell, D.W.2
  • 9
    • 0032551714 scopus 로고    scopus 로고
    • Association of Hsp105 with Hsc70 in high molecular mass complexes in mouse FM3A Cells
    • T. Hatayama, K. Yasuda, and K. Yasuda Association of Hsp105 with Hsc70 in high molecular mass complexes in mouse FM3A Cells Biochem. Biophys. Res. Commun. 248 1998 395 401
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 395-401
    • Hatayama, T.1    Yasuda, K.2    Yasuda, K.3
  • 10
    • 0242556837 scopus 로고    scopus 로고
    • Cytosolic Hsp90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
    • D.A. Hubert, P. Tornero, Y. Belkhadir, P. Krishna, A. Takahashi, K. Shirasu, and J.L. Dangl Cytosolic Hsp90 associates with and modulates the Arabidopsis RPM1 disease resistance protein EMBO J. 22 2003 5679 5689
    • (2003) EMBO J. , vol.22 , pp. 5679-5689
    • Hubert, D.A.1    Tornero, P.2    Belkhadir, Y.3    Krishna, P.4    Takahashi, A.5    Shirasu, K.6    Dangl, J.L.7
  • 11
    • 0029872081 scopus 로고    scopus 로고
    • The involvement of p23, Hsp90, and immunophilins in the assembly of progesterone receptor complexes
    • J. Johnson, R. Corbisier, B. Stensgard, and D. Toft The involvement of p23, Hsp90, and immunophilins in the assembly of progesterone receptor complexes J. Steroid Biochem. Mol. Biol. 56 1996 31 37
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.56 , pp. 31-37
    • Johnson, J.1    Corbisier, R.2    Stensgard, B.3    Toft, D.4
  • 12
    • 0031081435 scopus 로고    scopus 로고
    • Analysis of the native forms of the 90:kDa heat shock protein (Hsp90) in plant cytosolic extracts
    • P. Krishna, R.K. Reddy, M. Sacco, J.R. Frappier, and R.F. Felsheim Analysis of the native forms of the 90:kDa heat shock protein (Hsp90) in plant cytosolic extracts Plant Mol. Biol. 33 1997 457 466
    • (1997) Plant Mol. Biol. , vol.33 , pp. 457-466
    • Krishna, P.1    Reddy, R.K.2    Sacco, M.3    Frappier, J.R.4    Felsheim, R.F.5
  • 13
    • 0028675574 scopus 로고
    • A soybean 101-kDa heat shock protein complements a yeast Hsp104 deletion mutant in acquiring thermotolerance
    • Y.R.J. Lee, R.T. Nagao, and J.L. Key A soybean 101-kDa heat shock protein complements a yeast Hsp104 deletion mutant in acquiring thermotolerance Plant Cell 6 1994 1889 1897
    • (1994) Plant Cell , vol.6 , pp. 1889-1897
    • Lee, Y.R.J.1    Nagao, R.T.2    Key, J.L.3
  • 14
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabileEscherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • A. Mogk, T. Tomoyasu, P. Goloubinoff, S. Rudiger, D. Roder, and H. Langen Identification of thermolabileEscherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB EMBO J. 24 1999 934 6949
    • (1999) EMBO J. , vol.24 , pp. 934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6
  • 15
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones
    • K. Motohashi, Y. Watanabe, M. Yohda, and M. Yoshida Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones Proc. Natl. Acad. Sci. USA 96 1999 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
  • 16
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins: Estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor
    • S.C. Nair, E.J. Toran, R.A. Rimerman, S. Hjermstad, T.E. Smithgall, and D.F. Smith A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor Cell Stress Chaperon 4 1996 237 250
    • (1996) Cell Stress Chaperon , vol.4 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 18
    • 0033574756 scopus 로고    scopus 로고
    • Characterization of a maize heat-shock protein 101 gene, Hsp101, encoding a ClpB/Hsp100 protein homologue
    • J. Nieto-Sotelo, K.B. Kannan, L.M. Martinez, and C. Segal Characterization of a maize heat-shock protein 101 gene, Hsp101, encoding a ClpB/Hsp100 protein homologue Gene 230 1999 187 195
    • (1999) Gene , vol.230 , pp. 187-195
    • Nieto-Sotelo, J.1    Kannan, K.B.2    Martinez, L.M.3    Segal, C.4
  • 20
    • 0034694896 scopus 로고    scopus 로고
    • Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast
    • K. Okamura, Y. Kimata, H. Higashio, A. Tsuru, and K. Kohno Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast Biochem. Biophys. Res. Commun. 279 2000 445 450
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 445-450
    • Okamura, K.1    Kimata, Y.2    Higashio, H.3    Tsuru, A.4    Kohno, K.5
  • 21
    • 0029856744 scopus 로고    scopus 로고
    • Binding of immunophilins to the 90-kDa heat shock protein (Hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants
    • J.K. Owens-Grillo, L.F. Stancato, K. Hoffmann, W.B. Pratt, and P. Krishna Binding of immunophilins to the 90-kDa heat shock protein (Hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants Biochemistry 35 1996 15249 15255
    • (1996) Biochemistry , vol.35 , pp. 15249-15255
    • Owens-Grillo, J.K.1    Stancato, L.F.2    Hoffmann, K.3    Pratt, W.B.4    Krishna, P.5
  • 22
    • 0025815731 scopus 로고
    • Evidence that the 90-kDa Heat Shock (Hsp90) exists in cytosol in heteromeric complexes containing Hsp70 and three other proteins with Mr of 63,000, 56,0000, and 50,000
    • G.H. Perdew, and W.L. Whitelaw Evidence that the 90-kDa Heat Shock (Hsp90) exists in cytosol in heteromeric complexes containing Hsp70 and three other proteins with Mr of 63,000, 56,0000, and 50,000 J. Biol. Chem. 266 1991 6708 6713
    • (1991) J. Biol. Chem. , vol.266 , pp. 6708-6713
    • Perdew, G.H.1    Whitelaw, W.L.2
  • 23
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • W.B. Pratt, and D.O. Toft Steroid receptor interactions with heat shock protein and immunophilin chaperones Endocr. Rev. 18 1997 306 360
    • (1997) Endocr. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 24
    • 0032245891 scopus 로고    scopus 로고
    • High-molecular-weight FK506-binding proteins are components of heat-shock protein 90 heterocomplexes in wheat germ lysate
    • R.K. Reddy, I. Kurek, A.D. Silverstein, M. Chinkers, A. Breiman, and P. Krishna High-molecular-weight FK506-binding proteins are components of heat-shock protein 90 heterocomplexes in wheat germ lysate Plant Physiol. 118 1998 1395 1401
    • (1998) Plant Physiol. , vol.118 , pp. 1395-1401
    • Reddy, R.K.1    Kurek, I.2    Silverstein, A.D.3    Chinkers, M.4    Breiman, A.5    Krishna, P.6
  • 27
    • 0028675582 scopus 로고
    • An Arabidopsis heat shock protein complements a thermotolerance defect in yeast
    • E.C. Schirmer, S. Lindquist, and E. Vierling An Arabidopsis heat shock protein complements a thermotolerance defect in yeast Plant Cell 6 1994 1899 1909
    • (1994) Plant Cell , vol.6 , pp. 1899-1909
    • Schirmer, E.C.1    Lindquist, S.2    Vierling, E.3
  • 29
    • 0030448228 scopus 로고    scopus 로고
    • Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation
    • R. Schumacher, W. Hansen, B. Freeman, E. Alnemri, G. Litwack, and D. Toft Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation Biochemistry 35 1996 14889 14898
    • (1996) Biochemistry , vol.35 , pp. 14889-14898
    • Schumacher, R.1    Hansen, W.2    Freeman, B.3    Alnemri, E.4    Litwack, G.5    Toft, D.6
  • 30
    • 0026543821 scopus 로고
    • Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP-mediated events
    • D.F. Smith, B.A. Stensgard, W.J. Welch, and D.O. Toft Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP-mediated events J. Biol. Chem. 267 1992 1350 1356
    • (1992) J. Biol. Chem. , vol.267 , pp. 1350-1356
    • Smith, D.F.1    Stensgard, B.A.2    Welch, W.J.3    Toft, D.O.4
  • 32
    • 12044259947 scopus 로고
    • Steroid receptors and their associated proteins
    • D.F. Smith, and D.O. Toft Steroid receptors and their associated proteins Mol. Endocrinol. 7 1993 4 11
    • (1993) Mol. Endocrinol. , vol.7 , pp. 4-11
    • Smith, D.F.1    Toft, D.O.2
  • 33
    • 0030054166 scopus 로고    scopus 로고
    • Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with Hsp90
    • L.F. Stancato, K.A. Hutchsion, P. Krishna, and W.B. Pratt Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with Hsp90 Biochemistry 35 1996 554 561
    • (1996) Biochemistry , vol.35 , pp. 554-561
    • Stancato, L.F.1    Hutchsion, K.A.2    Krishna, P.3    Pratt, W.B.4
  • 34
    • 0029847609 scopus 로고    scopus 로고
    • Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate
    • V. Thulasiraman, and R. Matt Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate Biochemistry 35 1996 13443 13450
    • (1996) Biochemistry , vol.35 , pp. 13443-13450
    • Thulasiraman, V.1    Matt, R.2
  • 35
    • 0033970942 scopus 로고    scopus 로고
    • Characterization of native interaction of Hsp110 with Hsp25 and Hsc70
    • X.Y. Wang, X. Chen, H.J. Oh, E. Repasky, L. Kazim, and J. Subjeck Characterization of native interaction of Hsp110 with Hsp25 and Hsc70 FEBS Lett. 465 2000 98 102
    • (2000) FEBS Lett. , vol.465 , pp. 98-102
    • Wang, X.Y.1    Chen, X.2    Oh, H.J.3    Repasky, E.4    Kazim, L.5    Subjeck, J.6
  • 36
    • 0034724719 scopus 로고    scopus 로고
    • Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form
    • Y. Watanabe, K. Motohashi, M. Yohda, H. Taguchi, and M. Yoshida Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form J. Biol. Chem. 275 2000 12388 12392
    • (2000) J. Biol. Chem. , vol.275 , pp. 12388-12392
    • Watanabe, Y.1    Motohashi, K.2    Yohda, M.3    Taguchi, H.4    Yoshida, M.5
  • 37
    • 0029564092 scopus 로고
    • Cloning and expression of murine high mass heat shock proteins, Hsp105
    • K. Yasuda, A. Nakai, T. Hatayama, and K. Nagata Cloning and expression of murine high mass heat shock proteins, Hsp105 J. Biol. Chem. 270 1995 29718 29723
    • (1995) J. Biol. Chem. , vol.270 , pp. 29718-29723
    • Yasuda, K.1    Nakai, A.2    Hatayama, T.3    Nagata, K.4
  • 38
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ and GrpE in suppressing protein aggregation
    • M. Zolkiewski ClpB cooperates with DnaK, DnaJ and GrpE in suppressing protein aggregation J. Biol. Chem. 274 1999 28083 28086
    • (1999) J. Biol. Chem. , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.