References
Agterberg M, Adriaanse H, Tijhaar E, Resink A & Tommassen J (1989) Role of the cell surface-exposed regions of outer membrane protein PhoE ofEscherichia coli K-12 in the biogenesis of the protein. Eur. J. Biochem. 185: 365–370
Agterberg M, Adriaanse H, vanBruggen A, Karperien M & Tommassen J (1990) Outer membrane PhoE protein ofEscherichia coli K-12 as an exposure vector: possibilities and limitations. Gene 88: 37–45
Altman E, Kumamoto CA & Emr SD (1991) Heat-shock proteins can substitute for SecB function during protein export inEscherichia coli. EMBO J. 10: 239–245
Bernstein HD, Poritz MA, Strub K, Hoben PJ, Brenner S & Walter P (1989) Model for signal sequence recognition from amino acid sequence of 54K subunit of signal recognition particle. Nature 340: 482–486
Bochkareva ES, Lissin NM & Girshovich AS (1988) Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. Nature 336: 254–257
Bosch D, Leunissen J, Verbakel J, DeJong M, VanErp H & Tommassen J (1986) Periplasmic accumulation of truncated forms of outer membrane PhoE protein ofEscherichia coli K-12. J. Mol. Biol. 189: 449–455
Bosch D, Voorhout W & Tommassen J (1988) Export and localization of N-terminally truncated derivatives ofEscherichia coli K-12 outer membrane protein PhoE. J. Biol. Chem. 263: 9952–9957
Bosch D, Scholten M, Verhagen C & Tommassen J (1989) The role of the carboxy-terminal membrane-spanning fragment in the biogenesis ofEscherichia coli K-12 outer membrane protein PhoE. Mol. Gen. Genet. 216: 144–148
Brundage L, Hendrick JP, Schiebel E, Driessen AJM & Wickner W (1990) The purifiedE. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell 62: 649–657
Cabelli RJ, Chen L, Tai PC & Oliver DB (1988) SecA protein is required for secretory protein translocation intoE. coli membrave vesicles. Cell 55: 683–692
Collier DN, Bankaitis VA, Weiss JB & Bassford PJJr. (1988) The antifolding activity of SecB promotes the export of theE. coli maltose binding protein. Cell 53: 273–283
DeCock H, Hendriks R, DeVrije T & Tommassen J (1990a) Assembly of anin vitro synthesizedEscherichia coli outer membrane porin into its stable trimeric configuration. J. Biol. Chem. 265: 4646–4651
DeCock H, Hekstra D & Tommassen J (1990b)In vitro trimerization of outer membrane protein PhoE. Biochimie 72: 177–182
DeVrije T, DeSwart RL, Dowhan W, Tommassen J & DeKruijff B (1988) Phosphatidylglycerol is involved in protein translocation acrossEscherichia coli inner membranes. Nature 334: 173–175
Freudl R, Schwarz H, Klose M, Movva NR & Henning U (1985) The nature of information required for export and sorting, present within outer membrane protein OmpA ofEscherichia coli K-12. EMBO J. 4: 3593–3598
Klose M, Schwarz H, MacIntyre S, Freudl R, Eschbach M-L & Henning U (1988) Internal deletions in the gene for anEscherichia coli outer membrane protein define an area possibly important for recognition of the outer membrane by this polypeptide. J. Biol. Chem. 263: 13291–13296
Li P, Beckwith J & Inouye H (1988) Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely effect protein export inEscherichia coli. Proc. Natl. Acad. Sci. USA 85: 7685–7689
Lill R, Dowhan W & Wickner W (1990) The ATPase activity of SecA is regulated by acidic phospholipids, SecY and the leader and mature domains of precursor proteins. Cell 60: 271–280
Liu G, Topping TB & Randall LL (1989) Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein. Proc. Natl. Acad. Sci. USA 86: 9213–9217
MacIntyre S, Freudl R, Eschbach M-L & Henning U (1988) An artificial hydrophobic sequence functions as either an anchor or a signal sequence at only one of two positions within theEscherichia coli outer membrane protein OmpA. J. Biol. Chem. 263: 19053–19059
Moreno F, Fowler AV, Hall M, Silhavy TJ, Zabin I & Schwartz M (1980) A signal sequence is not sufficient to lead β-galacto-sidase out of the cytoplasm. Nature 286: 356–359
Nishiyama K, Kabuyama Y, Akimaru J, Matsuyama S, Tokuda H & Mizushima S (1991) SecY is an indispensable component of the protein secretory machinery ofEscherichia coli. Biochim. Biophys. Acta 1065: 89–97
Randall LL & Hardy SJS (1986) Correlation of competence for export with lack of tertiary structure of the mature species: a studyin vivo of maltose binding protein inE. coli. Cell 46: 921–928
Ribes V, Römisch K, Giner A, Dobberstein B & Tolervey D (1990)E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle. Cell 63: 591–600
Römisch K, Webb J, Herz J, Prehn S, Frank R, Vingron M & Dobberstein B (1989) Homology of 54K protein of signal recognition particle, docking protein and twoE. coli proteins with putative GTP binding domains. Nature 340: 478–482
Schatz PJ & Beckwith J (1990) Genetic analysis of protein export inEscherichia coli. Annu. Rev. Genet. 24: 215–248
Sen K & Nikaido H (1990)In vitro trimerization of OmpF porin secreted by spheroplasts ofEscherichia coli. Proc. Natl. Acad. Sci. USA 87: 743–747
Struyvé M, Moons M & Tommassen J (1991) Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J. Mol. Biol. 218: 141–148
Swidersky UA, Hoffschulte HK & Müller M (1990) Determinants of membrane targeting and transmembrane translocation during bacterial protein export. EMBO J. 9: 1777–1785
Tommassen J (1988) Biogenesis and membrane topology of outer membrane proteins inEscherichia coli. NATO ASI Series H 16: 351–373
Tommassen J, VanTol H & Lugtenberg B (1983) The ultimate localization of an outer membrane protein ofEscherichia coli K-12 is not determined by the signal sequence. EMBO J. 2: 1275–1279
Van derLey P, Struyvé M & Tommassen J (1986) Topology of outer membrane pore protein PhoE ofEscherichia coli. Identification of cell surface-exposed amino acids with the aid of monoclonal antibodies. J. Biol. Chem. 261: 12222–12225
Vogel H & Jähnig F (1986) Models for the structure of outer membrane proteins ofEscherichia coli derived from raman spectroscopy and prediction methods. J. Mol. Biol. 190: 191–199
Watanabe M & Blobel G (1989) SecB functions as a cytosolic signal recognition factor for protein export inE. coli. Cell 58: 695–705
Weiss JB, Ray PH & Bassford PJJr (1988) Purified SecB protein ofEscherichia coli retards folding and promotes membrane translocation of the maltose binding proteinin vitro. Proc. Natl. Acad. Sci. USA 85: 8978–8982
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Tommassen, J., Struyvé, M. & de Cock, H. Export and assembly of bacterial outer membrane proteins. Antonie van Leeuwenhoek 61, 81–85 (1992). https://doi.org/10.1007/BF00580611
Issue Date:
DOI: https://doi.org/10.1007/BF00580611