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PMID:337311

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Citation

Achtman, M, Kennedy, N and Skurray, R (1977) Cell--cell interactions in conjugating Escherichia coli: role of traT protein in surface exclusion. Proc. Natl. Acad. Sci. U.S.A. 74:5104-8

Abstract

Escherichia coli cells carrying the F sex factor are poor recipients in conjugation. This phenomenon is called surface exclusion. Two F cistrons, traS and traT, are independently responsible for part of the whole mechanism. The traS gene product reduces DNA transfer within stable mating aggregates. The traT gene product, pTraT, results in a greatly reduced ability to form stable mating aggregates, and thus also leads to reduced DNA transfer within the cell population. pTraT is a 25,000-dalton protein incorporated into the cell envelope outer membrane. It is found in 29,000-84,000 copies per cell, depending on the plasmid expressing it. There is a parallel variation in recipient ability. Models for surface exclusion are discussed.

Links

PubMed PMC432108

Keywords

Bacterial Proteins/biosynthesis; Bacterial Proteins/genetics; Cell Membrane/metabolism; Conjugation, Genetic; DNA, Bacterial/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/genetics; Membrane Proteins/biosynthesis; Membrane Proteins/genetics; Mutation

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:TRAT1

GO:0009279: cell outer membrane

ECO:0000314:

C

FIG. 4. Analysis of separated inner and outer membranes. Whole membranes (WM), outer membranes (OM), and inner membranes (IM) were isolated from cells carrying the plasmids indicated.

complete

ECOLI:TRAT1

GO:0031135: negative regulation of conjugation

ECO:0000315:

P

Table 1. The reduction in transfer efficiency relative to the control mating.

complete

ECOLI:TRAS1

GO:0031135: negative regulation of conjugation

ECO:0000315:

P

Table 1. Shows the reduction in transfer efficiency relative to the control mating

complete

ECOLI:TRAS1

GO:0016020: membrane

ECO:0000314:

C

Fig. 2. Gel electrophoresis of whole membrane preparations shows TraS.

complete


See also

References

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