Demonstration of a Folded Monomeric Form of Porin PhoE of Escherichia Coli in Vivo

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1996 Sep 1

PMID 8752355

Citations 10

Authors

P Van Gelder

J Tommassen

Affiliations

Soon will be listed here.

Abstract

The porins in the outer membranes of gram-negative bacteria are trimeric proteins. A folded monomeric form of the Escherichia coli porin PhoE, with a higher electrophoretic mobility than that of the denatured protein, has recently been detected in in vitro folding studies. To investigate the possible biological significance of the folded monomer, we attempted to detect this form in vivo. After pulse-labeling, folded monomers could be detected by immunoprecipitation. Furthermore, folded monomers were detected in a preparation of mutant PhoE porins, in which the subunit interactions were weakened by a E-66-->R substitution. Together, these results show that the folded monomer is not an in vitro folding artifact but an integral part of the native trimer.

Citing Articles

Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes.

Hussain S, Peterson J, Bernstein H mBio. 2021; 12(4):e0169621.

PMID: 34399610 PMC: 8406188. DOI: 10.1128/mBio.01696-21.

Weakly stable regions and protein-protein interactions in beta-barrel membrane proteins.

Naveed H, Liang J Curr Pharm Des. 2013; 20(8):1268-73.

PMID: 23713778 PMC: 4127314. DOI: 10.2174/13816128113199990071.

Structural basis for outer membrane sugar uptake in pseudomonads.

van den Berg B J Biol Chem. 2012; 287(49):41044-52.

PMID: 23066028 PMC: 3510807. DOI: 10.1074/jbc.M112.408518.

Engineered oligomerization state of OmpF protein through computational design decouples oligomer dissociation from unfolding.

Naveed H, Jimenez-Morales D, Tian J, Pasupuleti V, Kenney L, Liang J J Mol Biol. 2012; 419(1-2):89-101.

PMID: 22391420 PMC: 3772668. DOI: 10.1016/j.jmb.2012.02.043.

Predicting three-dimensional structures of transmembrane domains of β-barrel membrane proteins.

Naveed H, Xu Y, Jackups Jr R, Liang J J Am Chem Soc. 2011; 134(3):1775-81.

PMID: 22148174 PMC: 3415959. DOI: 10.1021/ja209895m.

References

Tommassen J, van Tol H, Lugtenberg B . The ultimate localization of an outer membrane protein of Escherichia coli K-12 is not determined by the signal sequence. EMBO J. 1983; 2(8):1275-9. PMC: 555272. DOI: 10.1002/j.1460-2075.1983.tb01581.x. View

Van Gelder P, de Cock H, Tommassen J . Detergent-induced folding of the outer-membrane protein PhoE, a pore protein induced by phosphate limitation. Eur J Biochem. 1994; 226(3):783-7. DOI: 10.1111/j.1432-1033.1994.00783.x. View

Heller K . Apparent molecular weights of a heat-modifiable protein from the outer membrane of Escherichia coli in gels with different acrylamide concentrations. J Bacteriol. 1978; 134(3):1181-3. PMC: 222370. DOI: 10.1128/jb.134.3.1181-1183.1978. View

Chai T, Foulds J . Two bacteriophages which utilize a new Escherichia coli major outer membrane protein as part of their receptor. J Bacteriol. 1978; 135(1):164-70. PMC: 224798. DOI: 10.1128/jb.135.1.164-170.1978. View

Towbin H, Staehelin T, Gordon J . Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979; 76(9):4350-4. PMC: 411572. DOI: 10.1073/pnas.76.9.4350. View

Tommassen J, Lugtenberg B . Outer membrane protein e of Escherichia coli K-12 is co-regulated with alkaline phosphatase. J Bacteriol. 1980; 143(1):151-7. PMC: 294200. DOI: 10.1128/jb.143.1.151-157.1980. View

van der Ley P, Amesz H, Tommassen J, Lugtenberg B . Monoclonal antibodies directed against the cell-surface-exposed part of PhoE pore protein of the Escherichia coli K-12 outer membrane. Eur J Biochem. 1985; 147(2):401-7. DOI: 10.1111/j.1432-1033.1985.tb08764.x. View

Nikaido H, Vaara M . Molecular basis of bacterial outer membrane permeability. Microbiol Rev. 1985; 49(1):1-32. PMC: 373015. DOI: 10.1128/mr.49.1.1-32.1985. View

Korteland J, Overbeeke N, de Graaff P, Overduin P, Lugtenberg B . Role of the Arg158 residue of the outer membrane PhoE pore protein of Escherichia coli K 12 in bacteriophage TC45 recognition and in channel characteristics. Eur J Biochem. 1985; 152(3):691-7. DOI: 10.1111/j.1432-1033.1985.tb09249.x. View

10.

Bosch D, Leunissen J, Verbakel J, de Jong M, van Erp H, Tommassen J . Periplasmic accumulation of truncated forms of outer-membrane PhoE protein of Escherichia coli K-12. J Mol Biol. 1986; 189(3):449-55. DOI: 10.1016/0022-2836(86)90316-5. View

11.

Stader J, Silhavy T . A progenitor of the outer membrane LamB trimer. J Bacteriol. 1988; 170(4):1973-4. PMC: 211062. DOI: 10.1128/jb.170.4.1973-1974.1988. View

12.

de Cock H, Hendriks R, de Vrije T, Tommassen J . Assembly of an in vitro synthesized Escherichia coli outer membrane porin into its stable trimeric configuration. J Biol Chem. 1990; 265(8):4646-51. View

13.

Agterberg M, Adriaanse H, Lankhof H, Meloen R, Tommassen J . Outer membrane PhoE protein of Escherichia coli as a carrier for foreign antigenic determinants: immunogenicity of epitopes of foot-and-mouth disease virus. Vaccine. 1990; 8(1):85-91. DOI: 10.1016/0264-410x(90)90184-n. View

14.

Schatz P, Beckwith J . Genetic analysis of protein export in Escherichia coli. Annu Rev Genet. 1990; 24:215-48. DOI: 10.1146/annurev.ge.24.120190.001243. View

15.

Sen K, Nikaido H . Trimerization of an in vitro synthesized OmpF porin of Escherichia coli outer membrane. J Biol Chem. 1991; 266(17):11295-300. View

16.

Misra R, Peterson A, Ferenci T, Silhavy T . A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. J Biol Chem. 1991; 266(21):13592-7. View

17.

Cowan S, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit R . Crystal structures explain functional properties of two E. coli porins. Nature. 1992; 358(6389):727-33. DOI: 10.1038/358727a0. View

18.

Ohmori H . A new method for strand discrimination in sequence-directed mutagenesis. Nucleic Acids Res. 1994; 22(5):884-5. PMC: 307898. DOI: 10.1093/nar/22.5.884. View

19.

Laird M, Kloser A, Misra R . Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12. J Bacteriol. 1994; 176(8):2259-64. PMC: 205347. DOI: 10.1128/jb.176.8.2259-2264.1994. View

20.

Lugtenberg B, Meijers J, Peters R, van der Hoek P, van Alphen L . Electrophoretic resolution of the "major outer membrane protein" of Escherichia coli K12 into four bands. FEBS Lett. 1975; 58(1):254-8. DOI: 10.1016/0014-5793(75)80272-9. View