메뉴 건너뛰기




Volumn 7, Issue 6, 1999, Pages

There's a right way and a wrong way: In vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 0033153294     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80078-1     Document Type: Review
Times cited : (67)

References (44)
  • 1
    • 1542563859 scopus 로고
    • Trimeric intermediate in the in vivo folding and subunit assembly pathways of the tailspike endorhamnosidase of bacteriophage P22
    • Goldenberg, D. & King, J. (1982). Trimeric intermediate in the in vivo folding and subunit assembly pathways of the tailspike endorhamnosidase of bacteriophage P22. Proc. Natl Acad. Sci. USA 79, 3403-3407.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 3403-3407
    • Goldenberg, D.1    King, J.2
  • 2
    • 0019429457 scopus 로고
    • Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein. III Inactive polypeptide chains synthesized at 39°C
    • Smith, D.H. & King, J. (1981). Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein. III Inactive polypeptide chains synthesized at 39°C. J. Mol. Biol. 145, 653-676.
    • (1981) J. Mol. Biol. , vol.145 , pp. 653-676
    • Smith, D.H.1    King, J.2
  • 3
    • 0011191567 scopus 로고
    • Genetic analysis of the folding pathway for the tail spike protein of phage P22
    • Goldenberg, D.P., Smith, D.H. & King, J. (1983). Genetic analysis of the folding pathway for the tail spike protein of phage P22. Proc. Natl Acad. Sci. USA 80, 7060-7064.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 7060-7064
    • Goldenberg, D.P.1    Smith, D.H.2    King, J.3
  • 4
    • 0024971016 scopus 로고
    • Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro
    • Seckler, R., Fuchs, A., King, J. & Jaenicke, R. (1989). Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro. J. Biol. Chem. 264, 11750-11753.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11750-11753
    • Seckler, R.1    Fuchs, A.2    King, J.3    Jaenicke, R.4
  • 5
    • 0030900095 scopus 로고    scopus 로고
    • Disulfide-bonded intermediate on the folding and assembly pathway of a non-disulfide bonded protein
    • Robinson, A.S. & King, J.A. (1997). Disulfide-bonded intermediate on the folding and assembly pathway of a non-disulfide bonded protein. Nat. Struct. Biol. 4, 450-455.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 450-455
    • Robinson, A.S.1    King, J.A.2
  • 6
    • 0028095571 scopus 로고
    • Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer
    • Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R. & Reinemer, P. (1994). Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer. Science 265, 383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 7
    • 0031564610 scopus 로고    scopus 로고
    • Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage
    • Steinbacher, S., et al., & Huber, R. (1997). Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage. J. Mol. Biol. 267, 865-880.
    • (1997) J. Mol. Biol. , vol.267 , pp. 865-880
    • Steinbacher, S.1    Huber, R.2
  • 8
    • 0029764093 scopus 로고    scopus 로고
    • Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors
    • Steinbacher, S., Baxa, U., Miller, S., Weintraub, A., Seckler, R. & Huber, R. (1996). Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. Proc. Natl Acad. Sci. USA 93, 10584-10588.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10584-10588
    • Steinbacher, S.1    Baxa, U.2    Miller, S.3    Weintraub, A.4    Seckler, R.5    Huber, R.6
  • 9
    • 0030918248 scopus 로고    scopus 로고
    • Interaction of Salmonella phage P22 with its O-antigen receptor studied by X-ray crystallography
    • Steinbacher, S., Miller, S., Baxa, U., Weintraub, A. & Seckler, R. (1997). Interaction of Salmonella phage P22 with its O-antigen receptor studied by X-ray crystallography. Biol. Chem. 378, 337-343.
    • (1997) Biol. Chem. , vol.378 , pp. 337-343
    • Steinbacher, S.1    Miller, S.2    Baxa, U.3    Weintraub, A.4    Seckler, R.5
  • 10
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder, M.D., Keen, N.T. & Jurnak, R. (1993). New domain motif: The structure of pectate lyase C, a secreted plant virulence factor. Science 260, 1503-1507.
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, R.3
  • 11
    • 0031688287 scopus 로고    scopus 로고
    • Structure and evolution of parallel beta-helix proteins
    • Jenkins, J., Mayans, O. & Pickersgill, R. (1998). Structure and evolution of parallel beta-helix proteins. J. Struct. Biol. 122, 236-246.
    • (1998) J. Struct. Biol. , vol.122 , pp. 236-246
    • Jenkins, J.1    Mayans, O.2    Pickersgill, R.3
  • 12
    • 0025228642 scopus 로고
    • Conformational stability of P22 tailspike proteins carrying temperature-sensitive folding mutations
    • Thomas, J., G.J., Becka, R., Sargent, D., Yu, M.-H. & King, J. (1990). Conformational stability of P22 tailspike proteins carrying temperature- sensitive folding mutations. Biochemistry 29, 4181-4187.
    • (1990) Biochemistry , vol.29 , pp. 4181-4187
    • Thomas, J.G.J.1    Becka, R.2    Sargent, D.3    Yu, M.-H.4    King, J.5
  • 13
    • 0019990304 scopus 로고
    • Maturation of the tailspike endrorhamnoside of Salmonella phage P22
    • Goldenberg, D., Berget, P. & King, J. (1982). Maturation of the tailspike endrorhamnoside of Salmonella phage P22. J. Biol. Chem 257, 7864-7871.
    • (1982) J. Biol. Chem , vol.257 , pp. 7864-7871
    • Goldenberg, D.1    Berget, P.2    King, J.3
  • 14
    • 0025821345 scopus 로고
    • In vitro folding pathway of phage P22 tailspike protein
    • Fuchs, A., Seiderer, C. & Seckler, R. (1991). In vitro folding pathway of phage P22 tailspike protein. Biochemistry 30, 6598-6604.
    • (1991) Biochemistry , vol.30 , pp. 6598-6604
    • Fuchs, A.1    Seiderer, C.2    Seckler, R.3
  • 15
    • 0027370268 scopus 로고
    • Mechanism of phage P22 tailspike protein folding mutations
    • Danner, M. & Seckler, R. (1993). Mechanism of phage P22 tailspike protein folding mutations. Protein Sci. 2, 1869-1881.
    • (1993) Protein Sci. , vol.2 , pp. 1869-1881
    • Danner, M.1    Seckler, R.2
  • 16
    • 0023883586 scopus 로고
    • Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. A model for inclusion body formation
    • Haase-Pettingell, C.A. & King, J. (1988). Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. A model for inclusion body formation. J. Biol. Chem. 263, 4977-4983.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4977-4983
    • Haase-Pettingell, C.A.1    King, J.2
  • 17
    • 0024978382 scopus 로고
    • Thermostability of temperature-sensitive folding mutants of the P22 tailspike protein
    • Sturtevant, J.M., Yu, M.-H., Haase-Pettingell, C. & King, J. (1989). Thermostability of temperature-sensitive folding mutants of the P22 tailspike protein. J. Biol. Chem. 264, 10693-10698.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10693-10698
    • Sturtevant, J.M.1    Yu, M.-H.2    Haase-Pettingell, C.3    King, J.4
  • 18
    • 0031854135 scopus 로고    scopus 로고
    • Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation
    • Betts, S.D. & King, J. (1998). Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off- pathway aggregation. Protein Sci. 7, 1516-1523.
    • (1998) Protein Sci. , vol.7 , pp. 1516-1523
    • Betts, S.D.1    King, J.2
  • 19
    • 0019474427 scopus 로고
    • Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30°C
    • Goldenberg, D.P. & King, J. (1981). Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30°C. J. Mol. Biol. 145, 633-651.
    • (1981) J. Mol. Biol. , vol.145 , pp. 633-651
    • Goldenberg, D.P.1    King, J.2
  • 20
    • 0024206047 scopus 로고
    • Nature and distribution of sites of temperature-sensitive folding mutations in the gene for the P22 tailspike polypeptide chain
    • Villafane, R. & King, J. (1988). Nature and distribution of sites of temperature-sensitive folding mutations in the gene for the P22 tailspike polypeptide chain. J. Mol. Biol. 204, 607-619.
    • (1988) J. Mol. Biol. , vol.204 , pp. 607-619
    • Villafane, R.1    King, J.2
  • 21
    • 0031582080 scopus 로고    scopus 로고
    • Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase
    • Haase-Pettingell, C. & King, J. (1997). Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase. J. Mol. Biol. 267, 88-102.
    • (1997) J. Mol. Biol. , vol.267 , pp. 88-102
    • Haase-Pettingell, C.1    King, J.2
  • 22
    • 0023834933 scopus 로고
    • Surface amino acids as sites of temperature-sensitive folding mutations in the P22 tailspike protein
    • Yu, M.H. & King, J. (1988). Surface amino acids as sites of temperature-sensitive folding mutations in the P22 tailspike protein. J. Biol. Chem. 263, 1424-1431.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1424-1431
    • Yu, M.H.1    King, J.2
  • 23
    • 0027321843 scopus 로고
    • Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro
    • Mitraki, A., Danner, M., King, J. & Seckler, R. (1993). Temperature- sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro. J. Biol. Chem. 268, 20071-20075.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20071-20075
    • Mitraki, A.1    Danner, M.2    King, J.3    Seckler, R.4
  • 24
  • 25
    • 0025968623 scopus 로고
    • Intragenic suppressors of folding defects in the P22 tailspike protein
    • Fane, B. & King, J. (1991). Intragenic suppressors of folding defects in the P22 tailspike protein. Genetics 127, 263-277.
    • (1991) Genetics , vol.127 , pp. 263-277
    • Fane, B.1    King, J.2
  • 26
    • 0026056333 scopus 로고
    • Identification of global suppressors for temperature-sensitive folding mutations of the P22 tailspike protein
    • Fane, B., Villafane, R., Mitraki, A. & King, J. (1991). Identification of global suppressors for temperature-sensitive folding mutations of the P22 tailspike protein. J. Biol. Chem. 261, 11640-11648.
    • (1991) J. Biol. Chem. , vol.261 , pp. 11640-11648
    • Fane, B.1    Villafane, R.2    Mitraki, A.3    King, J.4
  • 27
    • 0025850262 scopus 로고
    • Global suppression of protein folding defects and inclusion body formation
    • Mitraki, A., Fane, B., Haase-Pettingell, C., Sturtevant, J. & King, J. (1991). Global suppression of protein folding defects and inclusion body formation. Science 253, 54-58.
    • (1991) Science , vol.253 , pp. 54-58
    • Mitraki, A.1    Fane, B.2    Haase-Pettingell, C.3    Sturtevant, J.4    King, J.5
  • 28
    • 0026335389 scopus 로고
    • Molecular properties of global suppressors of temperature-sensitive folding mutations in P22 tailspike endorhamnosidase
    • Lee, S.C., Koh, H. & Yu, M.H. (1991). Molecular properties of global suppressors of temperature-sensitive folding mutations in P22 tailspike endorhamnosidase. J. Biol. Chem. 266, 23191-23196.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23191-23196
    • Lee, S.C.1    Koh, H.2    Yu, M.H.3
  • 29
    • 0032516802 scopus 로고    scopus 로고
    • P22 tailspike folding mutants revisited: Effects on the thermodynamic stability of the isolated beta-helix domain
    • In Process Citation
    • Schuler, B. & Seckler, R. (1998). P22 tailspike folding mutants revisited: Effects on the thermodynamic stability of the isolated beta- helix domain [In Process Citation]. J. Mol. Biol. 281, 227-234.
    • (1998) J. Mol. Biol. , vol.281 , pp. 227-234
    • Schuler, B.1    Seckler, R.2
  • 30
    • 0027165264 scopus 로고
    • Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain
    • Danner, M., Fuchs, A., Miller, S. & Seckler, R. (1993). Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain. Eur. J. Biochem. 215, 653-661.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 653-661
    • Danner, M.1    Fuchs, A.2    Miller, S.3    Seckler, R.4
  • 31
    • 0027509618 scopus 로고
    • Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro
    • Brunschier, R., Danner, M. & Seckler, R. (1993). Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro. J. Biol. Chem. 268, 2767-2772.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2767-2772
    • Brunschier, R.1    Danner, M.2    Seckler, R.3
  • 32
    • 0028943183 scopus 로고
    • Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains
    • Speed, M.A., Wang, D.I. & King, J. (1995). Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains. Protein Sci. 4, 900-908.
    • (1995) Protein Sci. , vol.4 , pp. 900-908
    • Speed, M.A.1    Wang, D.I.2    King, J.3
  • 33
    • 0031021542 scopus 로고    scopus 로고
    • Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies
    • Speed, M.A., Morshead, T., Wang, D.I. & King, J. (1997). Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Protein Sci. 6, 99-108.
    • (1997) Protein Sci. , vol.6 , pp. 99-108
    • Speed, M.A.1    Morshead, T.2    Wang, D.I.3    King, J.4
  • 34
    • 0032884679 scopus 로고    scopus 로고
    • Detection of early aggregation intermediates using native gel electrophoresis and native western blotting
    • in press
    • Betts, S.D., Speed, M.A. & King, J.A. (1999). Detection of early aggregation intermediates using native gel electrophoresis and native western blotting. Methods Enzymol. 307, in press.
    • (1999) Methods Enzymol. , vol.307
    • Betts, S.D.1    Speed, M.A.2    King, J.A.3
  • 35
    • 0030943938 scopus 로고    scopus 로고
    • Monitoring the refolding pathway for a large multimeric protein using capillary zone electrophoresis
    • Fan, Z.H., Jensen, P.K., Lee, C.S. & King, J. (1997). Monitoring the refolding pathway for a large multimeric protein using capillary zone electrophoresis. J. Chromatogr. 669, 315-323.
    • (1997) J. Chromatogr. , vol.669 , pp. 315-323
    • Fan, Z.H.1    Jensen, P.K.2    Lee, C.S.3    King, J.4
  • 36
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
    • Speed, M.A., Wang, D.I.C. & King, J. (1996). Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Nat. Biotech. 14, 1283-1287.
    • (1996) Nat. Biotech. , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.C.2    King, J.3
  • 37
    • 0028036622 scopus 로고
    • Intracellular trapping of a cytoplasmic folding intermediate of the phage P22 tailspike using iodoacetamide
    • Sather, S.K. & King, J. (1994). Intracellular trapping of a cytoplasmic folding intermediate of the phage P22 tailspike using iodoacetamide. J. Biol. Chem. 269, 25268-25276.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25268-25276
    • Sather, S.K.1    King, J.2
  • 38
    • 0028004372 scopus 로고
    • Selective in vivo rescue by GroEl-ES of thermolabile folding intermediate to phage P22 structural proteins
    • Gordon, C.L., Sather, S.K., Casjens, S. & King, J. (1994). Selective in vivo rescue by GroEl-ES of thermolabile folding intermediate to phage P22 structural proteins. J. Biol. Chem. 269, 27941-27951.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27941-27951
    • Gordon, C.L.1    Sather, S.K.2    Casjens, S.3    King, J.4
  • 39
    • 0025301071 scopus 로고
    • Properties of monoclonal antibodies selected for probing the conformation of wild type and mutant forms of the P22 tailspike endorhamnosidase
    • Friguet, B., Djavadi-Ohaniance, L., Haase-Pettingell, C.A., King, J. & Goldberg, M.E. (1990). Properties of monoclonal antibodies selected for probing the conformation of wild type and mutant forms of the P22 tailspike endorhamnosidase. J. Biol. Chem. 265, 10347-10351.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10347-10351
    • Friguet, B.1    Djavadi-Ohaniance, L.2    Haase-Pettingell, C.A.3    King, J.4    Goldberg, M.E.5
  • 40
    • 0028300803 scopus 로고
    • In vitro and ribosome-bound folding intermediates of P22 tailspike protein detected with monoclonal antibodies
    • Friguet, B., Djavadi-Ohaniance, L., King, J. & Goldberg, M.E. (1994). In vitro and ribosome-bound folding intermediates of P22 tailspike protein detected with monoclonal antibodies. J. Biol. Chem. 269, 15945-15949.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15945-15949
    • Friguet, B.1    Djavadi-Ohaniance, L.2    King, J.3    Goldberg, M.E.4
  • 41
    • 0029653878 scopus 로고
    • Nascent chains: Folding and chaperone interaction during elongation on ribosomes
    • Tokatlidis, K., et al., & Goldberg, M.E. (1995). Nascent chains: Folding and chaperone interaction during elongation on ribosomes. Philos. Trans. R. Soc. Lond. B Biol. Sci. 348, 89-95.
    • (1995) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.348 , pp. 89-95
    • Tokatlidis, K.1    Goldberg, M.E.2
  • 42
    • 0032560643 scopus 로고    scopus 로고
    • A reversibly unfolding fragment of P22 tailspike protein with native structure: The isolated beta-helix domain
    • Miller, S., Schuler, B. & Seckler, R. (1998). A reversibly unfolding fragment of P22 tailspike protein with native structure: The isolated beta-helix domain. Biochemistry 37, 9160-9168.
    • (1998) Biochemistry , vol.37 , pp. 9160-9168
    • Miller, S.1    Schuler, B.2    Seckler, R.3
  • 43
    • 0025867101 scopus 로고
    • Thermal unfolding pathway for the thermostable P22 endorhamnosidase
    • Chen, B.L. & King, J. (1991). Thermal unfolding pathway for the thermostable P22 endorhamnosidase. Biochemistry 30, 6260-6269.
    • (1991) Biochemistry , vol.30 , pp. 6260-6269
    • Chen, B.L.1    King, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.