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Gene Review:

tlpA - alpha-helical coiled-coil protein

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

Hurme, R. et al., Koski, P. et al., Hyman, H.C. et al.

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Disease relevance of tlpA

Salmonella cells shifted to higher temperatures, such as those encountered at host entry, showed derepressed tlpA activity. tlpA::lacZ fusions indicated that the promoter itself is insensitive to thermal shifts and that transcription control was exerted by the autorepressor TlpA only [1].

High impact information on tlpA

The gene (tlpA) encoding this protein (TlpA) was isolated from the large virulence-associated plasmid of S. typhimurium and sequenced in order to predict the primary structure of TlpA. tlpA encodes a 371-amino acid soluble protein with a calculated M(r) of 41600 and pI of 4.63 [2].
The resulting amino acid substitutions are near the C terminus predicted to form an alpha-helical coiled coil [3].

References

A proteinaceous gene regulatory thermometer in Salmonella. Hurme, R., Berndt, K.D., Normark, S.J., Rhen, M. Cell (1997) [Pubmed]
A new alpha-helical coiled coil protein encoded by the Salmonella typhimurium virulence plasmid. Koski, P., Saarilahti, H., Sukupolvi, S., Taira, S., Riikonen, P., Osterlund, K., Hurme, R., Rhen, M. J. Biol. Chem. (1992) [Pubmed]
Point mutations that lock Salmonella typhimurium flagellar filaments in the straight right-handed and left-handed forms and their relation to filament superhelicity. Hyman, H.C., Trachtenberg, S. J. Mol. Biol. (1991) [Pubmed]

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