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Review
. 2000 Sep;182(18):5029-35.
doi: 10.1128/JB.182.18.5029-5035.2000.

Vectorial metabolism and the evolution of transport systems

M H Saier Jr  1
Affiliations
Review

Vectorial metabolism and the evolution of transport systems

M H Saier Jr. J Bacteriol. 2000 Sep.
No abstract available

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Figures

FIG. 1
FIG. 1
Illustration of a chemical transformation reaction involving a group transfer process. D, donor; A, acceptor; G, group transferred. (Reproduced from reference with permission.)
FIG. 2
FIG. 2
Illustration of enzyme-catalyzed group translocation as proposed by Peter Mitchell. ATP and ADP, adenosine tri- and diphosphates; P, phosphoryl group; S, substrate. (Reproduced from reference with permission.)
FIG. 3
FIG. 3
Models of recognized classes of transporters. (a) Proteinaceous channel-mediated passive diffusion (e.g., the glycerol facilitator of E. coli, GlpF) of a substrate (●) across the cytoplasmic membrane of a gram-negative bacterial cell. (b) Carrier-mediated solute-H+ symport (e.g., the lactose permease of E. coli). (c) Carrier-mediated symport using an extracytoplasmic receptor (a solute binding protein [BP]) to confer high-affinity solute recognition (e.g., the DctMPQ dicarboxylate TRAP transporter of R. capsulatus. (d) ATP hydrolysis-driven primary active uptake via an ABC transporter (e.g., the maltose permease of E. coli). (e) A group-translocating permease of the PTS in which sugar is concomitantly transported and phosphorylated in a coupled process in which Enzyme I (EI), HPr, IIA, and IIB are sequentially phosphorylated in preparation for sugar transport and phosphorylation (e.g., the glucose permease of E. coli). PEP, phosphoenolpyruvate; P, phosphoryl group. (Reproduced from reference with permission.)
FIG. 4
FIG. 4
Depiction of three independent pathways for the evolution of six- and seven-TMS transporter modules. A, MC family of exchange transporters; B, MIP family of aquaporins and glycerol facilitators; C, LCT family of eukaryotic organellar proteins. Arrows indicate the direction of passage through the membrane, while numbers refer to the TMSs in the repeat unit of the polypeptide chain.
FIG. 5
FIG. 5
Illustration of three independent duplication events that gave rise to current 12-TMS (or 14-TMS) transporter polypeptide chains. A, MFS; B, RND superfamily; C, PET family.
FIG. 6
FIG. 6
Proposed pathway for the construction of present-day TRAP-T and ArsAB family permeases. The presumed precursor transporter was a single 12-TMS secondary transporter in both cases, but auxiliary proteins were superimposed upon them during evolution to confer either high-affinity substrate recognition (TRAP-T) or ATP hydrolysis-driven energy coupling (ARS).
FIG. 7
FIG. 7
Illustration of the overall geometry and features of the catalytic events for the Na+-transporting oxaloacetate decarboxylase. B-H, biotin; B-CO2−, carboxybiotin; Lys, biotin-binding residue; 1, carboxyltransferase reaction; 2, decarboxylase reaction. The α subunit catalyzes decarboxylation, the β subunit catalyzes transport, and the γ subunit is proposed to facilitate linkage of these two subunits into a single membrane-embedded protein complex. (Reproduced from reference with permission.)
FIG. 8
FIG. 8
Schematic depiction of four E. coli (E.c.) PTS permeases, those specific for mannitol (Mtl, top), glucose (Glc), cellobiose (Cel), and mannose (Man, bottom). Abbreviations of the proteins are as follows: I, Enzyme I; H, HPr; IIA, IIB, and IIC, the three functionally distinct domains of the Enzyme II complexes; IID, an extra domain found only in the mannose permease. The scheme illustrates the coupling of phosphoryl transfer from phosphoenolpyruvate (PEP) through various protein intermediates to give cytoplasmic sugar-phosphate (P) from exogenous sugars.
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