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Fluorescein Analogues Inhibit SecA ATPase: The First Sub‐micromolar Inhibitor of Bacterial Protein Translocation
Author(s) -
Huang YingJu,
Wang Hongyun,
Gao FenBiao,
Li Minyong,
Yang Hsiuchin,
Wang Binghe,
Tai Phang C.
Publication year - 2012
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201100594
Subject(s) - chromosomal translocation , fluorescein , atpase , chemistry , biochemistry , biophysics , microbiology and biotechnology , biology , fluorescence , enzyme , gene , physics , quantum mechanics
Abstract SecA is a central component of the general secretion system that is essential for bacterial growth and thus an ideal target for antimicrobial agents. A series of fluorescein analogues were first screened against the ATPase activity using the truncated unregulated SecA catalytic domain. Rose bengal (RB) and erythrosin B (EB) were found to be potent inhibitors SecA with IC 50 values of 0.5 μ M and 2 μ M , respectively. RB and EB inhibit the catalytic SecA ATPase more effectively than the F 1 F 0 ‐proton ATPase. We used three assays to test the effect of these compounds on full‐length SecA ATPase: in solution (intrinsic ATPase), in membrane preparation, and translocation ATPase. RB and EB show the following trend in terms of IC 50 values: translocation ATPase