메뉴 건너뛰기




Volumn 584, Issue 16, 2010, Pages 3620-3624

Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli

Author keywords

Chaperone; Luciferase; Multi domain; Ribosome; Trigger factor

Indexed keywords

BACTERIAL ENZYME; CHAPERONE; ESCHERICHIA COLI PROTEIN; LUCIFERASE; PROTEIN PPIASE; TRIGGER FACTOR; UNCLASSIFIED DRUG;

EID: 77955655122     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.07.036     Document Type: Article
Times cited : (17)

References (27)
  • 1
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl F.U., Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 2009, 16:574-581.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 2
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22:1399-1408.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 3
    • 25144498144 scopus 로고    scopus 로고
    • De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria
    • Chang H.C., Kaiser C.M., Hartl F.U., Barral J.M. De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria. J. Mol. Biol. 2005, 353:397-409.
    • (2005) J. Mol. Biol. , vol.353 , pp. 397-409
    • Chang, H.C.1    Kaiser, C.M.2    Hartl, F.U.3    Barral, J.M.4
  • 4
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer W.J., Hartl F.U. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature 1997, 388:343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 5
    • 1942421714 scopus 로고    scopus 로고
    • Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed
    • Agashe V.R., et al. Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed. Cell 2004, 117:199-209.
    • (2004) Cell , vol.117 , pp. 199-209
    • Agashe, V.R.1
  • 6
    • 77649272553 scopus 로고    scopus 로고
    • Slowing bacterial translation speed enhances eukaryotic protein folding efficiency
    • Siller E., DeZwaan D.C., Anderson J.F., Freeman B.C., Barral J.M. Slowing bacterial translation speed enhances eukaryotic protein folding efficiency. J. Mol. Biol. 2010, 396:1310-1318.
    • (2010) J. Mol. Biol. , vol.396 , pp. 1310-1318
    • Siller, E.1    DeZwaan, D.C.2    Anderson, J.F.3    Freeman, B.C.4    Barral, J.M.5
  • 7
    • 11444271010 scopus 로고    scopus 로고
    • Chaperone-assisted folding of newly synthesized proteins in the cytosol
    • Deuerling E., Bukau B. Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit. Rev. Biochem. Mol. Biol. 2004, 39:261-277.
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 261-277
    • Deuerling, E.1    Bukau, B.2
  • 8
    • 58749091073 scopus 로고    scopus 로고
    • Chaperone over-expression in Escherichia coli: apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates
    • Haacke A., Fendrich G., Ramage P., Geiser M. Chaperone over-expression in Escherichia coli: apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates. Protein Expr. Purif. 2009, 64:185-193.
    • (2009) Protein Expr. Purif. , vol.64 , pp. 185-193
    • Haacke, A.1    Fendrich, G.2    Ramage, P.3    Geiser, M.4
  • 9
    • 0035807963 scopus 로고    scopus 로고
    • Binding specificity of Escherichia coli trigger factor
    • Patzelt H., et al. Binding specificity of Escherichia coli trigger factor. Proc. Natl. Acad. Sci. USA 2001, 98:14244-14249.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14244-14249
    • Patzelt, H.1
  • 11
    • 0037068441 scopus 로고    scopus 로고
    • L23 protein functions as a chaperone docking site on the ribosome
    • Kramer G., et al. L23 protein functions as a chaperone docking site on the ribosome. Nature 2002, 419:171-174.
    • (2002) Nature , vol.419 , pp. 171-174
    • Kramer, G.1
  • 12
    • 33646343968 scopus 로고    scopus 로고
    • Alternate recruitment of signal recognition particle and trigger factor to the signal sequence of a growing nascent polypeptide
    • Eisner G., Moser M., Schafer U., Beck K., Muller M. Alternate recruitment of signal recognition particle and trigger factor to the signal sequence of a growing nascent polypeptide. J. Biol. Chem. 2006, 281:7172-7179.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7172-7179
    • Eisner, G.1    Moser, M.2    Schafer, U.3    Beck, K.4    Muller, M.5
  • 13
    • 33744925719 scopus 로고    scopus 로고
    • Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle
    • Ullers R.S., Houben E.N., Brunner J., Oudega B., Harms N., Luirink J. Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle. J. Biol. Chem. 2006, 281:13999-14005.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13999-14005
    • Ullers, R.S.1    Houben, E.N.2    Brunner, J.3    Oudega, B.4    Harms, N.5    Luirink, J.6
  • 14
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides
    • Valent Q.A., Kendall D.A., High S., Kusters R., Oudega B., Luirink J. Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 1995, 14:5494-5505.
    • (1995) EMBO J. , vol.14 , pp. 5494-5505
    • Valent, Q.A.1    Kendall, D.A.2    High, S.3    Kusters, R.4    Oudega, B.5    Luirink, J.6
  • 15
    • 44649188719 scopus 로고    scopus 로고
    • Molecular mechanism and structure of trigger factor bound to the translating ribosome
    • Merz F., et al. Molecular mechanism and structure of trigger factor bound to the translating ribosome. EMBO J. 2008, 27:1622-1632.
    • (2008) EMBO J. , vol.27 , pp. 1622-1632
    • Merz, F.1
  • 16
    • 4944246094 scopus 로고    scopus 로고
    • Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
    • Ferbitz L., Maier T., Patzelt H., Bukau B., Deuerling E., Ban N. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 2004, 431:590-596.
    • (2004) Nature , vol.431 , pp. 590-596
    • Ferbitz, L.1    Maier, T.2    Patzelt, H.3    Bukau, B.4    Deuerling, E.5    Ban, N.6
  • 17
    • 24744435971 scopus 로고    scopus 로고
    • Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action
    • Baram D., Pyetan E., Sittner A., Auerbach-Nevo T., Bashan A., Yonath A. Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action. Proc. Natl. Acad. Sci. USA 2005, 102:12017-12022.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12017-12022
    • Baram, D.1    Pyetan, E.2    Sittner, A.3    Auerbach-Nevo, T.4    Bashan, A.5    Yonath, A.6
  • 18
    • 34249691985 scopus 로고    scopus 로고
    • Identification of nascent chain interaction sites on trigger factor
    • Lakshmipathy S.K., et al. Identification of nascent chain interaction sites on trigger factor. J. Biol. Chem. 2007, 282:12186-12193.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12186-12193
    • Lakshmipathy, S.K.1
  • 19
    • 33845984939 scopus 로고    scopus 로고
    • The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity
    • Merz F., Hoffmann A., Rutkowska A., Zachmann-Brand B., Bukau B., Deuerling E. The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity. J. Biol. Chem. 2006, 281:31963-31971.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31963-31971
    • Merz, F.1    Hoffmann, A.2    Rutkowska, A.3    Zachmann-Brand, B.4    Bukau, B.5    Deuerling, E.6
  • 20
    • 73949113446 scopus 로고    scopus 로고
    • Chaperone domains convert prolyl isomerases into generic catalysts of protein folding
    • Jakob R.P., Zoldak G., Aumuller T., Schmid F.X. Chaperone domains convert prolyl isomerases into generic catalysts of protein folding. Proc. Natl. Acad. Sci. USA 2009, 106:20282-20287.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20282-20287
    • Jakob, R.P.1    Zoldak, G.2    Aumuller, T.3    Schmid, F.X.4
  • 21
    • 0031029046 scopus 로고    scopus 로고
    • Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
    • Scholz C., Stoller G., Zarnt T., Fischer G., Schmid F.X. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 1997, 16:54-58.
    • (1997) EMBO J. , vol.16 , pp. 54-58
    • Scholz, C.1    Stoller, G.2    Zarnt, T.3    Fischer, G.4    Schmid, F.X.5
  • 23
    • 1842639447 scopus 로고    scopus 로고
    • Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli
    • Kramer G., Patzelt H., Rauch T., Kurz T.A., Vorderwulbecke S., Bukau B., Deuerling E. Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. J. Biol. Chem. 2004, 279:14165-14170.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14165-14170
    • Kramer, G.1    Patzelt, H.2    Rauch, T.3    Kurz, T.A.4    Vorderwulbecke, S.5    Bukau, B.6    Deuerling, E.7
  • 24
    • 0031543319 scopus 로고    scopus 로고
    • A set of pBR322-compatible plasmids allowing the testing of chaperone-assisted folding of proteins overexpressed in Escherichia coli
    • Castanie M.P., Berges H., Oreglia J., Prere M.F., Fayet O. A set of pBR322-compatible plasmids allowing the testing of chaperone-assisted folding of proteins overexpressed in Escherichia coli. Anal. Biochem. 1997, 254:150-152.
    • (1997) Anal. Biochem. , vol.254 , pp. 150-152
    • Castanie, M.P.1    Berges, H.2    Oreglia, J.3    Prere, M.F.4    Fayet, O.5
  • 26
    • 77955659939 scopus 로고    scopus 로고
    • Versatility of trigger factor interactions with ribosome-nascent chain complexes
    • doi: doi:10.1074/jbc.M110.134163, (M110.134163 First Published on July 1, 2010).
    • Lakshmipathy, S.K., Gupta, R., Pinkert, S., Etchells, S.A. and Hartl, F.U. (2010) Versatility of trigger factor interactions with ribosome-nascent chain complexes. J. Biol. Chem. doi: (M110.134163 First Published on July 1, 2010). doi:10.1074/jbc.M110.134163.
    • (2010) J. Biol. Chem.
    • Lakshmipathy, S.K.1    Gupta, R.2    Pinkert, S.3    Etchells, S.A.4    Hartl, F.U.5
  • 27
    • 0032983520 scopus 로고    scopus 로고
    • Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    • Frydman J., Erdjument-Bromage H., Tempst P., Hartl F.U. Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase. Nat. Struct. Biol. 1999, 6:697-705.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 697-705
    • Frydman, J.1    Erdjument-Bromage, H.2    Tempst, P.3    Hartl, F.U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.