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Volumn 180, Issue 6, 1998, Pages 1396-1401

Identification of a sequence motif that confers SecB dependence on a SecB-independent secretory protein in vivo

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; CHAPERONE; MALTOSE BINDING PROTEIN; MUTANT PROTEIN; SECRETORY PROTEIN;

EID: 0031893538     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.6.1396-1401.1998     Document Type: Article
Times cited : (21)

References (47)
  • 1
    • 0025999145 scopus 로고
    • Recognition of a protein translocation system containing purified SecY, SecE, and Seca from Escherichia coli
    • Akimaru, J., S. Matsuyama, H. Tokuda, and S. Mizushima. 1991. Recognition of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli. Proc. Natl. Acad. Sci. USA 88:6545-6549.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6545-6549
    • Akimaru, J.1    Matsuyama, S.2    Tokuda, H.3    Mizushima, S.4
  • 2
    • 0025166042 scopus 로고
    • The presence of both the signal sequence and a region of mature LamB protein is required for the interaction of LamB with the export factor SecB
    • Altman, E., S. D. Emr, and C. A. Kumamoto. 1990. The presence of both the signal sequence and a region of mature LamB protein is required for the interaction of LamB with the export factor SecB. J. Biol. Chem. 265:18154-18168.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18154-18168
    • Altman, E.1    Emr, S.D.2    Kumamoto, C.A.3
  • 3
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein, H. D., M. A. Poritz, K. Strub, P. J. Hoben, S. Brenner, and P. Walter. 1989. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340:482-486.
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 4
    • 0025087853 scopus 로고
    • The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation
    • Brundage, L., J. P. Hendrick, E. Schiebel, A. J. M. Driessen, and W. Wickner. 1990. The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell 62:649-657.
    • (1990) Cell , vol.62 , pp. 649-657
    • Brundage, L.1    Hendrick, J.P.2    Schiebel, E.3    Driessen, A.J.M.4    Wickner, W.5
  • 5
    • 0028935007 scopus 로고
    • The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: Evidence for an electrophoresis-like membrane transfer mechanism
    • Cao, G., A. Kuhn, and R. E. Dalbey. 1995. The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: evidence for an electrophoresis-like membrane transfer mechanism. EMBO J. 14:866-875.
    • (1995) EMBO J. , vol.14 , pp. 866-875
    • Cao, G.1    Kuhn, A.2    Dalbey, R.E.3
  • 6
    • 0029060799 scopus 로고
    • Artificial transmembrane segments
    • Chen, H., and D. A. Kendall. 1995. Artificial transmembrane segments. J. Biol. Chem. 270:14115-14122.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14115-14122
    • Chen, H.1    Kendall, D.A.2
  • 7
    • 0029830550 scopus 로고    scopus 로고
    • Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway
    • Chen, H., J. Kim, and D. A. Kendall. 1996. Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway. J. Bacteriol. 178:6658-6664.
    • (1996) J. Bacteriol. , vol.178 , pp. 6658-6664
    • Chen, H.1    Kim, J.2    Kendall, D.A.3
  • 9
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • Economou, A., and W. Wickner. 1994. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78:835-843.
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 10
    • 0012295328 scopus 로고
    • Purification of microsomal signal peptidase as a complex
    • Evans, E. A., R. Gilmore, and G. Blobel. 1986. Purification of microsomal signal peptidase as a complex. Proc. Natl. Acad. Sci. USA 83:581-585.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 581-585
    • Evans, E.A.1    Gilmore, R.2    Blobel, G.3
  • 11
    • 0030703175 scopus 로고    scopus 로고
    • The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation
    • Fekkes, P., C. van der Does, and A. J. M. Driessen. 1997. The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. EMBO J. 16:6105-6113.
    • (1997) EMBO J. , vol.16 , pp. 6105-6113
    • Fekkes, P.1    Van Der Does, C.2    Driessen, A.J.M.3
  • 12
    • 0024614332 scopus 로고
    • The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export
    • Gannon, P. M., P. Li, and C. A. Kumamoto. 1989. The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export. J. Bacteriol. 171:813-818.
    • (1989) J. Bacteriol. , vol.171 , pp. 813-818
    • Gannon, P.M.1    Li, P.2    Kumamoto, C.A.3
  • 13
    • 0025045470 scopus 로고
    • The secD locus of E. coli codes for two membrane proteins required for protein export
    • Gardel, C., K. Johnson, A. Jacq, and J. Beckwith. 1990. The secD locus of E. coli codes for two membrane proteins required for protein export. EMBO J. 9:3209-3216.
    • (1990) EMBO J. , vol.9 , pp. 3209-3216
    • Gardel, C.1    Johnson, K.2    Jacq, A.3    Beckwith, J.4
  • 14
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • Hartl, F. U., S. Lecker, E. Schiebel, J. P. Hendrick, and W. Wickner. 1990. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell 63:269-279.
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.U.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.P.4    Wickner, W.5
  • 15
    • 0029810395 scopus 로고    scopus 로고
    • The amino-terminal charge and core region hydrophobicity interdependently contribute to the function of signal sequences
    • Izard, J. W., S. L. Rusch, and D. A. Kendall. 1996. The amino-terminal charge and core region hydrophobicity interdependently contribute to the function of signal sequences. J. Biol. Chem. 271:21579-21582.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21579-21582
    • Izard, J.W.1    Rusch, S.L.2    Kendall, D.A.3
  • 16
    • 0026501333 scopus 로고
    • In vitro translocation of secretory proteins possessing no charges at the mature domain takes place efficiently in a proton motive force-dependent manner
    • Kato, M., H. Tokuda, and S. Mizushima. 1992. In vitro translocation of secretory proteins possessing no charges at the mature domain takes place efficiently in a proton motive force-dependent manner. J. Biol. Chem. 267: 413-418.
    • (1992) J. Biol. Chem. , vol.267 , pp. 413-418
    • Kato, M.1    Tokuda, H.2    Mizushima, S.3
  • 17
    • 0023047564 scopus 로고
    • Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide
    • Kendall, D. A., S. C. Bock, and E. T. Kaiser. 1986. Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide. Nature (London) 321:706-708.
    • (1986) Nature (London) , vol.321 , pp. 706-708
    • Kendall, D.A.1    Bock, S.C.2    Kaiser, E.T.3
  • 18
    • 0024296720 scopus 로고
    • A functional decaisoleucine-containing signal sequence
    • Kendall, D. A., and E. T. Kaiser. 1988. A functional decaisoleucine-containing signal sequence. J. Biol. Chem. 263:7261-7265.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7261-7265
    • Kendall, D.A.1    Kaiser, E.T.2
  • 19
    • 0028875765 scopus 로고
    • Mapping of the binding frame for the chaperone SecB within a natural ligand, galactose-binding protein
    • Khisty, V. J., G. R. Munske, and L. L. Randall. 1995. Mapping of the binding frame for the chaperone SecB within a natural ligand, galactose-binding protein. J. Biol. Chem. 270:25920-25927.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25920-25927
    • Khisty, V.J.1    Munske, G.R.2    Randall, L.L.3
  • 20
    • 0026700218 scopus 로고
    • Involvement of SecB, a chaperone, in the export of ribose-binding protein
    • Kim, J., Y. Lee, C. Kim, and C. Park. 1992. Involvement of SecB, a chaperone, in the export of ribose-binding protein. J. Bacteriol. 174:5219-5227.
    • (1992) J. Bacteriol. , vol.174 , pp. 5219-5227
    • Kim, J.1    Lee, Y.2    Kim, C.3    Park, C.4
  • 21
  • 22
    • 0027956170 scopus 로고
    • SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state
    • Kim, Y. J., T. Rajapandi, and D. Oliver. 1994. SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state. Cell 78:845-853.
    • (1994) Cell , vol.78 , pp. 845-853
    • Kim, Y.J.1    Rajapandi, T.2    Oliver, D.3
  • 23
    • 0029128122 scopus 로고
    • Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB
    • Kimsey, H. H., M. D. Dagarag, and C. A. Kumamoto. 1995. Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB. J. Biol. Chem. 270:22831-22835.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22831-22835
    • Kimsey, H.H.1    Dagarag, M.D.2    Kumamoto, C.A.3
  • 24
    • 0026013244 scopus 로고
    • Molecular chaperones and protein translocation across the Escherichia coli inner membrane
    • Kumamoto, C. A. 1991. Molecular chaperones and protein translocation across the Escherichia coli inner membrane. Mol. Microbiol. 5:19-22.
    • (1991) Mol. Microbiol. , vol.5 , pp. 19-22
    • Kumamoto, C.A.1
  • 25
    • 0021867206 scopus 로고
    • Evidence for specificity at an early step in protein export in Escherichia coli
    • Kumamoto, C. A., and J. Beckwith. 1985. Evidence for specificity at an early step in protein export in Escherichia coli. J. Bacteriol. 163:267-274.
    • (1985) J. Bacteriol. , vol.163 , pp. 267-274
    • Kumamoto, C.A.1    Beckwith, J.2
  • 26
    • 0024790857 scopus 로고
    • SecB protein stabilizes a translocation-competent state of purified prePhoE protein
    • Kusters, R., T. de Vrije, E. Breukink, and B. de Kruijff. 1989. SecB protein stabilizes a translocation-competent state of purified prePhoE protein. J. Biol. Chem. 264:20827-20830.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20827-20830
    • Kusters, R.1    De Vrije, T.2    Breukink, E.3    De Kruijff, B.4
  • 27
    • 0024461843 scopus 로고
    • Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli
    • Kusukawa, N., T. Yura, C. Ueguchi, Y. Akiyama, and K. Ito. 1989. Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli. EMBO J. 8:3517-3521.
    • (1989) EMBO J. , vol.8 , pp. 3517-3521
    • Kusukawa, N.1    Yura, T.2    Ueguchi, C.3    Akiyama, Y.4    Ito, K.5
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0025967209 scopus 로고
    • Functional limits of conformation, hydrophobicity, and steric constraints in prokaryotic signal peptidc cleavage regions
    • Laforet, G. A., and D. A. Kendall. 1991. Functional limits of conformation, hydrophobicity, and steric constraints in prokaryotic signal peptidc cleavage regions. J. Biol. Chem. 266:1326-1334.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1326-1334
    • Laforet, G.A.1    Kendall, D.A.2
  • 30
    • 0027458691 scopus 로고
    • SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli
    • Matsuyama, S., Y. Fujita, and S. Mizushima. 1993. SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli. EMBO J. 12:265-270.
    • (1993) EMBO J. , vol.12 , pp. 265-270
    • Matsuyama, S.1    Fujita, Y.2    Mizushima, S.3
  • 31
  • 32
    • 0029997381 scopus 로고    scopus 로고
    • Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation
    • Nishiyama, K., T. Suzuki, and H. Tokuda. 1996. Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell 85:71-81.
    • (1996) Cell , vol.85 , pp. 71-81
    • Nishiyama, K.1    Suzuki, T.2    Tokuda, H.3
  • 33
    • 0027455603 scopus 로고
    • SecA protein: Autoregulated ATPase catalysing preprotein insertion and translocation across the Escherichia coli inner membrane
    • Oliver, D. B. 1993. SecA protein: autoregulated ATPase catalysing preprotein insertion and translocation across the Escherichia coli inner membrane. Mol. Microbiol. 7:159-165.
    • (1993) Mol. Microbiol. , vol.7 , pp. 159-165
    • Oliver, D.B.1
  • 34
    • 0025087137 scopus 로고
    • Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery
    • Oliver, D. B., R. J. Cabelli, K. M. Dolan, and G. P. Jarosik. 1990. Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery. Proc. Natl. Acad. Sci. USA 87:8227-8231.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8227-8231
    • Oliver, D.B.1    Cabelli, R.J.2    Dolan, K.M.3    Jarosik, G.P.4
  • 35
    • 0023882692 scopus 로고
    • Modulation of folding pathways of exported proteins by the leader sequence
    • Park, S., G. Liu, T. B. Topping, W. H. Cover, and L. L. Randall. 1988. Modulation of folding pathways of exported proteins by the leader sequence. Science 239:1033-1035.
    • (1988) Science , vol.239 , pp. 1033-1035
    • Park, S.1    Liu, G.2    Topping, T.B.3    Cover, W.H.4    Randall, L.L.5
  • 36
    • 0026794697 scopus 로고
    • The E. coli ffh gene is necessary for viability and efficient protein export
    • Phillips, G. J., and T. J. Silhavy. 1992. The E. coli ffh gene is necessary for viability and efficient protein export. Nature 359:744-746.
    • (1992) Nature , vol.359 , pp. 744-746
    • Phillips, G.J.1    Silhavy, T.J.2
  • 37
    • 0025605808 scopus 로고
    • An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle
    • Poritz, M. A., H. D. Bernstein, K. Strub, D. Zopf, H. Wilhelm, and P. Walter. 1990. An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle. Science 250:1111-1117.
    • (1990) Science , vol.250 , pp. 1111-1117
    • Poritz, M.A.1    Bernstein, H.D.2    Strub, K.3    Zopf, D.4    Wilhelm, H.5    Walter, P.6
  • 38
    • 0026755898 scopus 로고
    • Peptide binding by chaperone SecB: Implications for recognition of nonnative structure
    • Randall, L. L. 1992. Peptide binding by chaperone SecB: implications for recognition of nonnative structure. Science 257:241-245.
    • (1992) Science , vol.257 , pp. 241-245
    • Randall, L.L.1
  • 39
    • 0025315285 scopus 로고
    • No specific recognition of leader peptide by SecB, a chaperone involved in protein export
    • Randall, L. L., T. B. Topping, and S. J. S. Hardy. 1990. No specific recognition of leader peptide by SecB, a chaperone involved in protein export. Science 248:860-863.
    • (1990) Science , vol.248 , pp. 860-863
    • Randall, L.L.1    Topping, T.B.2    Hardy, S.J.S.3
  • 40
    • 0028282428 scopus 로고
    • Signal peptide hydrophobicity is finely tailored for function
    • Rusch, S. L., H. Chen, J. W. Izard, and D. A. Kendall. 1994. Signal peptide hydrophobicity is finely tailored for function. J. Cell. Biochem. 55:209-217.
    • (1994) J. Cell. Biochem. , vol.55 , pp. 209-217
    • Rusch, S.L.1    Chen, H.2    Izard, J.W.3    Kendall, D.A.4
  • 42
    • 0027486004 scopus 로고
    • Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli
    • Strobel, S. M., J. G. Cannon, and P. J. Bassford, Jr. 1993. Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coli. J. Bacteriol. 175:6988-6995.
    • (1993) J. Bacteriol. , vol.175 , pp. 6988-6995
    • Strobel, S.M.1    Cannon, J.G.2    Bassford Jr., P.J.3
  • 43
    • 0028214003 scopus 로고
    • Determination of the binding frame within a physiological ligand for the chaperone SecB
    • Topping, T. B., and L. L. Randall. 1994. Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Sci. 3:730-736.
    • (1994) Protein Sci. , vol.3 , pp. 730-736
    • Topping, T.B.1    Randall, L.L.2
  • 44
    • 0031472242 scopus 로고    scopus 로고
    • The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
    • Ulbrandt, N. D., J. A. Newitt, and H. D. Bernstein. 1997. The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 88:187-196.
    • (1997) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 45
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides
    • Valent, Q. A., D. A. Kendall, S. High, R. Kusters, B. Oudega, and J. Luirink. 1995. Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 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
  • 46
    • 0024411967 scopus 로고
    • SecB functions as a cytosolic signal recognition factor for protein export in E. coli
    • Watanabe, M., and G. Blobel. 1989. SecB functions as a cytosolic signal recognition factor for protein export in E. coli. Cell 58:695-705.
    • (1989) Cell , vol.58 , pp. 695-705
    • Watanabe, M.1    Blobel, G.2
  • 47
    • 0023795525 scopus 로고
    • Synthesis and export of the outer membrane lipoprotein in Escherichia coli mutants defective in generalized protein export
    • Watanabe, T., S. Hayashi, and H. C. Wu. 1988. Synthesis and export of the outer membrane lipoprotein in Escherichia coli mutants defective in generalized protein export. J. Bacteriol. 170:4001-4007.
    • (1988) J. Bacteriol. , vol.170 , pp. 4001-4007
    • Watanabe, T.1    Hayashi, S.2    Wu, H.C.3


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