Ontology highlight
ABSTRACT:
SUBMITTER: Steinbrecher T
PROVIDER: S-EPMC3471478 | biostudies-literature | 2012 Oct
REPOSITORIES: biostudies-literature
Steinbrecher Thomas T Prock Sebastian S Reichert Johannes J Wadhwani Parvesh P Zimpfer Benjamin B Bürck Jochen J Berditsch Marina M Elstner Marcus M Ulrich Anne S AS
Biophysical journal 20121002 7
The bacterial stress-response peptide TisB in Escherichia coli has been suggested to dissipate the transmembrane potential, such that the depletion of ATP levels induces the formation of dormant persister cells which can eventually form biofilms. We studied the structure and membrane interactions of TisB to find out whether it forms pores or other proton-selective channels. Circular dichroism revealed an amphiphilic α-helical structure when reconstituted in lipid vesicles, and oriented circular ...[more]