Detection of a Protein, Similar to the Sex Pilus Subunit, in the Outer Membrane of Escherichia Coli Cells Carrying a Derepressed F-like R Factor

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1975 Apr 1

PMID 1091630

Citations 23

Authors

J P Beard

J C Connolly

Affiliations

Soon will be listed here.

Abstract

The outer membranes of Escherichia coli K-12 cells carrying a derepressed F-like R factor contain about 7 times 10-4 molecules per cell of a protein similar to the subunit of the sex pili specified by the R factor. This protein pool is absent in cells carrying the repressed variant of the R factor. The size of the pool is about one-half of the amount of protein incorporated into mature sex pili at the peak of production and is independent of the phase of growth of the culture. The molecular weight of the protein in the pool and of the subunit of the sex pili specified by the cells is 12,500 plus or minus 600.

Citing Articles

Molecular cloning and functional characterization of a copy number control gene (copB) of plasmid R1.

Riise E, Stougaard P, Bindslev B, Nordstrom K, Molin S J Bacteriol. 1982; 151(3):1136-45.

PMID: 7050078 PMC: 220389. DOI: 10.1128/jb.151.3.1136-1145.1982.

Expression of a copy number control gene (copB) of plasmid R1 is constitutive and growth rate dependent.

Light J, Molin S J Bacteriol. 1982; 151(3):1129-35.

PMID: 7050077 PMC: 220388. DOI: 10.1128/jb.151.3.1129-1135.1982.

Replication control functions of plasmid R1 act as inhibitors of expression of a gene required for replication.

Light J, Molin S Mol Gen Genet. 1981; 184(1):56-61.

PMID: 7038389 DOI: 10.1007/BF00271195.

Runaway replication of plasmid R1 is not caused by loss of replication inhibitor activity of gene cop.

Molin S, Diaz R, Uhlin B, Nordstrom K J Bacteriol. 1980; 143(2):1046-8.

PMID: 7009544 PMC: 294415. DOI: 10.1128/jb.143.2.1046-1048.1980.

Control of plasmid R1 replication: functions involved in replication, copy number control, incompatibility, and switch-off of replication.

Molin S, Nordstrom K J Bacteriol. 1980; 141(1):111-20.

PMID: 6986353 PMC: 293542. DOI: 10.1128/jb.141.1.111-120.1980.

References

Burton K . A study of the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochem J. 1956; 62(2):315-23. PMC: 1215910. DOI: 10.1042/bj0620315. View

GOA J . A micro biuret method for protein determination; determination of total protein in cerebrospinal fluid. Scand J Clin Lab Invest. 1953; 5(3):218-22. DOI: 10.3109/00365515309094189. View

LOWRY O, ROSEBROUGH N, FARR A, RANDALL R . Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193(1):265-75. View

BRINTON Jr C . The properties of sex pili, the viral nature of "conjugal" genetic transfer systems, and some possible approaches to the control of bacterial drug resistance. CRC Crit Rev Microbiol. 1971; 1(1):105-60. DOI: 10.3109/10408417109104479. View

Novotny C, Lavin K . Some effects of temperature on the growth of F pili. J Bacteriol. 1971; 107(3):671-82. PMC: 246987. DOI: 10.1128/jb.107.3.671-682.1971. View

Beard J, Howe T, Richmond M . Purification of sex pili from Escherichia coli carrying a derepressed F-like R factor. J Bacteriol. 1972; 111(3):814-20. PMC: 251357. DOI: 10.1128/jb.111.3.814-820.1972. View

Grinsted J, Saunders J, Ingram L, Sykes R, Richmond M . Properties of a R factor which originated in Pseudomonas aeruginosa 1822. J Bacteriol. 1972; 110(2):529-37. PMC: 247445. DOI: 10.1128/jb.110.2.529-537.1972. View

Fairbanks G, Steck T, Wallach D . Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971; 10(13):2606-17. DOI: 10.1021/bi00789a030. View

Bosch V, Braun V . Distribution of murein-lipoprotein between the cytoplasmic and outer membrane of Escherichia coli. FEBS Lett. 1973; 34(2):307-10. DOI: 10.1016/0014-5793(73)80818-x. View

10.

Braun V, Gnirke H, Henning U, Rehn K . Model for the structure of the shape-maintaining layer of the Escherichia coli cell envelope. J Bacteriol. 1973; 114(3):1264-70. PMC: 285390. DOI: 10.1128/jb.114.3.1264-1270.1973. View

11.

AMES G, Spudich E, Nikaido H . Protein composition of the outer membrane of Salmonella typhimurium: effect of lipopolysaccharide mutations. J Bacteriol. 1974; 117(2):406-16. PMC: 285527. DOI: 10.1128/jb.117.2.406-416.1974. View

12.

Holland I, Tuckett S . Study of envelope proteins in E. coli cet and recA mutants by SDS acrylamide gel electrophoresis. J Supramol Struct. 1972; 1(2):77-97. DOI: 10.1002/jss.400010202. View

13.

Costerton J, Ingram J, Cheng K . Structure and function of the cell envelope of gram-negative bacteria. Bacteriol Rev. 1974; 38(1):87-110. PMC: 413842. DOI: 10.1128/br.38.1.87-110.1974. View

14.

Beard J, Howe T, Richmond M . Centrifugation properties of sex pili. J Mol Biol. 1972; 66(2):311-3. DOI: 10.1016/0022-2836(72)90483-4. View

15.

Osborn M, Gander J, Parisi E, Carson J . Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J Biol Chem. 1972; 247(12):3962-72. View

16.

Novotny C, Raizen E, Knight W, BRINTON Jr C . Functions of F pili in mating-pair formation and male bacteriophage infection studies by blending spectra and reappearance kinetics. J Bacteriol. 1969; 98(3):1307-19. PMC: 315328. DOI: 10.1128/jb.98.3.1307-1319.1969. View

17.

MEYNELL E, Meynell G, Datta N . Phylogenetic relationships of drug-resistance factors and other transmissible bacterial plasmids. Bacteriol Rev. 1968; 32(1):55-83. PMC: 378292. DOI: 10.1128/br.32.1.55-83.1968. View

18.

BRINTON Jr C . The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in gram negative bacteria. Trans N Y Acad Sci. 1965; 27(8):1003-54. DOI: 10.1111/j.2164-0947.1965.tb02342.x. View

19.

Lawn A, MEYNELL E, Cooke M . Mixed infections with bacterial sex factors: sex pili of pure and mixed phenotype. Ann Inst Pasteur (Paris). 1971; 120(1):3-8. View

20.

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View