YehZYXW of Escherichia coli Is a Low-Affinity, Non-Osmoregulatory Betaine-Specific ABC Transporter

Biochemistry
Shenhui LangJanet M Wood

Abstract

Transporter-mediated osmolyte accumulation stimulates the growth of Escherichia coli in high-osmolality environments. YehZYXW was predicted to be an osmoregulatory transporter because (1) osmotic and stationary phase induction of yehZYXW is mediated by RpoS, (2) the Yeh proteins are homologous to the components of known osmoregulatory ABC transporters (e.g., ProU of E. coli), and (3) YehZ models based on the structures of periplasmic betaine-binding proteins suggested that YehZ retains key betaine-binding residues. The betaines choline-O-sulfate, glycine betaine, and dimethylsulfoniopropionate bound YehZ and ProX with millimolar and micromolar affinities, respectively, as determined by equilibrium dialysis and isothermal titration calorimetry. The crystal structure of the YehZ apoprotein, determined at 1.5 Å resolution (PDB ID: 4WEP ), confirmed its similarity to other betaine-binding proteins. Small and nonpolar residues in the hinge region of YehZ (e.g., Gly223) pack more closely than the corresponding residues in ProX, stabilizing the apoprotein. Betaines bound YehZ-Gly223Ser an order of magnitude more tightly than YehZ, suggesting that weak substrate binding in YehZ is at least partially due to apo state stabilization. Neit...Continue Reading

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Citations

Dec 3, 2016·Nucleic Acids Research·Ingrid M KeselerPeter D Karp
Apr 11, 2018·Acta Crystallographica. Section F, Structural Biology Communications·Jian Hong ZhaoYong Xing He
Aug 12, 2018·Applied and Environmental Microbiology·Laura TeichmannErhard Bremer
Nov 9, 2018·Frontiers in Microbiology·Stefanie RonzheimerErhard Bremer
May 7, 2021·Journal of Molecular Biology·Marco van den NoortBert Poolman
Dec 9, 2021·Archives of Microbiology·Sébastien Bontemps-GalloFlorent Sebbane

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