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Author Mousa, Jarrod J. ♦ Newsome, Rachel C. ♦ Yang, Ye ♦ Jobin, Christian ♦ Bruner, Steven D.
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword APPLIED LIFE SCIENCES ♦ CATIONS ♦ ESCHERICHIA COLI ♦ MOLECULES ♦ TOXICITY ♦ X RADIATION
Abstract Multidrug transporters play key roles in cellular drug resistance to toxic molecules, yet these transporters are also involved in natural product transport as part of biosynthetic clusters in bacteria and fungi. The genotoxic molecule colibactin is produced by strains of virulent and pathobiont Escherichia coli and Klebsiella pneumoniae. In the biosynthetic cluster is a multidrug and toxic compound extrusion protein (MATE) proposed to transport the prodrug molecule precolibactin across the cytoplasmic membrane, for subsequent cleavage by the peptidase ClbP and cellular export. We recently determined the X-ray structure of ClbM, and showed preliminary data suggesting its specific role in precolibactin transport. Here, we define a functional role of ClbM by examining transport capabilities under various biochemical conditions. Our data indicate ClbM responds to sodium, potassium, and rubidium ion gradients, while also having substantial transport activity in the absence of alkali cations. - Highlights: • ClbM is a cation promiscuous MATE multidrug transporter. • The role of key residues were identified in both the cation and proton binding. • The biologically relevant substrate for ClbM is the natural product precolibactin.
ISSN 0006291X
Educational Use Research
Learning Resource Type Article
Publisher Date 2017-01-22
Publisher Place United States
Journal Biochemical and Biophysical Research Communications
Volume Number 482
Issue Number 4


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