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| Content Provider | PubMed Central |
|---|---|
| Author | Nakayama, Jiro Takanami, Yuuichiro Horii, Takaaki Sakuda, Shohei Suzuki, Akinori |
| Copyright Year | 1998 |
| Abstract | Conjugative transfer of the Enterococcus faecalis plasmid pPD1 is activated by cPD1, one of several peptide sex pheromones secreted by plasmid-free recipient cells, and is blocked by a donor-produced peptide inhibitor, iPD1. Using a tritiated pheromone, [3H]cPD1, we investigated how pPD1-harboring donor cells receive these peptide signals. Donor cells rapidly incorporated [3H]cPD1. The cell extract but not the membrane fraction of the donor strain exhibited significant [3H]cPD1-binding activity. On the basis of these data and those of tracer studies, it was demonstrated that cPD1 was internalized, where it bound to a high-molecular-weight compound. The cell extract of a strain carrying the traA-bearing multicopy plasmid (pDLHH21) also exhibited high [3H]cPD1-binding activity. A recombinant TraA exhibited a dissociation constant of 0.49 ± 0.08 nM against [3H]cPD1. iPD1 competitively inhibited [3H]cPD1 binding to TraA, whereas pheromones and inhibitors relating to other plasmid systems did not. These results show that TraA is a specific intracellular receptor for cPD1 and that iPD1 acts as an antagonist for TraA. A strain carrying the traC-bearing multicopy plasmid (pDLES23) exhibited significant [3H]cPD1-binding activity. A strain carrying traC-disrupted pPD1 (pAM351CM) exhibited lower [3H]cPD1-binding activity as well as lower sensitivity to cPD1 than a wild-type donor strain. Some of the other pheromones and inhibitors inhibited [3H]cPD1 binding to the traC transformant like cPD1 and iPD1 did. These results show that TraC, as an extracellular less-specific pheromone-binding protein, supports donor cells to receive cPD1. |
| Starting Page | 449 |
| File Format | |
| ISSN | 10985530 |
| e-ISSN | 10985530 |
| Journal | Journal of Bacteriology |
| Issue Number | 3 |
| Volume Number | 180 |
| Language | English |
| Publisher | American Society for Microbiology |
| Publisher Date | 1998-02-01 |
| Access Restriction | Open |
| Rights Holder | American Society for Microbiology |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Molecular Biology Microbiology |
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