Transient receptor potential (TRP) genes encode a family of related ion-channel subunits. This family consists of cationselective, calcium-permeable channels that include a group of vanilloid receptor channels (TRPV) implicated in pain and inflammation. These channels are activated by diverse stimuli, including capsaicin, lipids, membrane deformation, heat, and protons. Six members of the TRPV family have been identified that differ predominantly in their activation properties. However, in neurons, TRPV channels do not account for the observed diversity of responses to activators. By probing human and rat brain cDNA libraries to identify TRPV subunits, we identified a novel human TRPV1 RNA splice variant, TRPV1b, which forms functional ion channels that are activated by temperature (threshold, ϳ47°C), but not by capsaicin or protons. Channels with similar activation properties were found in trigeminal ganglion neurons, suggesting that TRPV1b receptors are expressed in these cells and contribute to thermal nociception.

The broad-host-range plasmid R1162 is conjugally mobilized at high frequency by the IncP-1 plasmid R751 but is poorly mobilized by pOX38, a derivative of the F factor. In both cases, the origin of transfer (oriT) and the Mob proteins of R1162 are required, indicating that these plasmids are mobilized by similar mechanisms. R1162 encodes a primase, essential for vegetative replication of the plasmid, that is made both as a separate protein and as the carboxy-terminal domain of MobA, one of the R1162 mobilization proteins (P. Scholz, V. Haring, B. Wittman-Liebold, K. Ashman, M. Bagdasarian, and E. Scherzinger, Gene 75:271-288, 1989). When R751 is the mobilizing vector, the primase is not required for mobilization of plasmids containing cloned mob-oriT R1162 DNA. However, detectable mobilization of such plasmids by pOX38 requires both the primase and its cognate initiation site, oriented for synthesis of the complement to the transferred strand. The long form of the primase is required for optimal transfer: R1162 replicons lacking this form also are not transferred detectably by pOX38 and are less well mobilized by R751. The distance between oriT and the primase initiation site affects the frequency of mobilization, and this effect is polar in the direction of transfer. Our results indicate that the R1162 primase is active in mobilization of R1162 and suggest that the MobA-linked form is an adaptation increasing its effectiveness during transfer.

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Cells newly transformed with plasmid R1162 DNA were used as donors in conjugal matings to determine if the plasmid replication genes are necessary for transfer. An intact system for vegetative replication is not required for transfer at normal frequency, but the plasmid primase, in the form linked to the nickase, must be present in donor cells.

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