Altered oxyanion selectivity in mutants of UhpT, the Pi-linked sugar phosphate carrier of Escherichia coli

Jason A. Hall, Peter C. Maloney

Research output: Contribution to journalArticle

Abstract

In Escherichia coli, the UhpT transporter catalyzes the electroneutral accumulation of sugar 6-phosphate by exchange with internal inorganic phosphate (Pi). The substrate specificity of UhpT is regulated at least in part by constituents of an Asp388-Lys391 intrahelical salt bridge, and mutations that remove one but not both of these residues alter UhpT preference for organophosphate substrates. Using site-directed mutagenesis, we examined the role played by these two positions in the selection of the oxyanion countersubstrate. We show that derivatives having aliphatic or polar residues at positions 388 and 391 are gain-of-function mutants capable of transporting SO4 as well as Pi. These oxyanions share similar structures but differ significantly in the presence of a proton(s) on P i. Our findings therefore lead us to suggest that the Asp 388-Lys391 ion pair acts normally as a filter that prevents substrates lacking a proton that can be donated from occupying the UhpT active site.

Original languageEnglish (US)
Pages (from-to)3376-3381
Number of pages6
JournalJournal of Biological Chemistry
Volume280
Issue number5
DOIs
StatePublished - Feb 4 2005

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Phosphate Transport Proteins
Sugar Phosphates
Escherichia coli
Protons
Organophosphates
Substrates
Substrate Specificity
Site-Directed Mutagenesis
Phosphates
Catalytic Domain
Mutagenesis
Salts
Ions
Sugars
Mutation
Derivatives

ASJC Scopus subject areas

  • Biochemistry

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Altered oxyanion selectivity in mutants of UhpT, the Pi-linked sugar phosphate carrier of Escherichia coli. / Hall, Jason A.; Maloney, Peter C.

In: Journal of Biological Chemistry, Vol. 280, No. 5, 04.02.2005, p. 3376-3381.

Research output: Contribution to journalArticle

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