A proteinaceous gene regulatory thermometer in Salmonella
1997 (English)In: Cell, ISSN 0092-8674, E-ISSN 1097-4172, Vol. 90, no 1, 55-64 p.Article in journal (Refereed) PublishedText
Novel utilization of the coiled-coil motif is presented that enables TlpA, an autoregulatory repressor protein in Salmonella, to sense temperature shifts directly and thereby to modulate the extent of transcription repression. 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. In vitro studies with highly purified TlpA showed concentration and temperature dependence for both fully folded conformation and function, indicating that the thermosensing in TlpA is based on monomer-to-coiled-coil equilibrium.
Place, publisher, year, edition, pages
1997. Vol. 90, no 1, 55-64 p.
DNA-binding, environmental-regulation, escherichia-coli, heat-shock, helical coiled-coils, pathogenic bacteria, shigella-flexneri, shock transcription factor-1, smooth-muscle tropomyosin, temperature regulation
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:sh:diva-29021DOI: 10.1016/S0092-8674(00)80313-XISI: A1997XL36200008PubMedID: 9230302ScopusID: 2-s2.0-0031472233OAI: oai:DiVA.org:sh-29021DiVA: diva2:891681
Times Cited: 35 Article English Cited References Count: 63 Xl3622016-01-072016-01-072016-01-11Bibliographically approved