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. 1990 Mar;54(1):1–17. doi: 10.1128/mr.54.1.1-17.1990

Anion-exchange mechanisms in bacteria.

P C Maloney 1, S V Ambudkar 1, V Anatharam 1, L A Sonna 1, A Varadhachary 1
PMCID: PMC372756  PMID: 2181257

Abstract

This article discusses the physiological, biochemical, and molecular properties of bacterial anion-exchange reactions, with a particular focus on a family of phosphate (Pi)-linked antiporters that accept as their primary substrates sugar phosphates such as glucose 6-phosphate (G6P), mannose 6-phosphate, or glycerol 3-phosphate. Pi-linked antiporters may be found in both gram-positive and gram-negative cells. As their name suggests, these exchange proteins accept both inorganic and organic phosphates, but the two classes of substrate interact very differently with the protein. Thus, Pi is always accepted with a relatively low affinity, and when it participates in exchange, it is always taken as the monovalent anion. By contrast, when the high-affinity organic phosphates are used, these same systems fail to discriminate between monovalent and divalent forms. Tests of heterologous exchange (e.g., Pi: G6P) indicate that these proteins have a bifunctional active site that accepts a pair of negative charges, whether as two monovalent anions or as a single divalent anion. For this reason, exchange stoichiometry moves between limits of 2:1 and 2:2, according to the ratio of mono- and divalent substrates at either membrane surface. Since G6P has a pK2 within the physiological range (pK of 6.1), this predicts a novel reaction sequence in vivo because internal pH is more alkaline than external pH. Accordingly, one expects an asymmetric exchange as two monovalent G6P anions from the relatively acidic exterior move against a single divalent G6P from the alkaline interior. In this way an otherwise futile self-exchange of G6P can be biased towards a net inward flux driven (indirectly) by the pH gradient. Despite the biochemical complexity exhibited by Pi-linked antiporters, they resemble all other secondary carriers at a molecular level and show a likely topology in which two sets of six transmembrane alpha-helices are connected by a central hydrophilic loop. Speculations on the derivation of this common form suggest a limited number of structural models to accommodate such proteins. Three such models are presented.

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Selected References

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