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Journal of Bacteriology, August 2002, p. 4071-4080, Vol. 184, No. 15
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.15.4071-4080.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Rhizobium leguminosarum Has a Second General Amino Acid Permease with Unusually Broad Substrate Specificity and High Similarity to Branched-Chain Amino Acid Transporters (Bra/LIV) of the ABC Family

School of Animal and Microbial Sciences, University of Reading, Reading RG6 6AJ, United Kingdom

Received 12 February 2002/ Accepted 2 May 2002

Amino acid uptake by Rhizobium leguminosarum is dominated by two ABC transporters, the general amino acid permease (Aap) and the branched-chain amino acid permease (Bra_Rl). Characterization of the solute specificity of Bra_Rl shows it to be the second general amino acid permease of R. leguminosarum. Although Bra_Rl has high sequence identity to members of the family of hydrophobic amino acid transporters (HAAT), it transports a broad range of solutes, including acidic and basic polar amino acids (L-glutamate, L-arginine, and L-histidine), in addition to neutral amino acids (L-alanine and L-leucine). While amino and carboxyl groups are required for transport, solutes do not have to be -amino acids. Consistent with this, Bra_Rl is the first ABC transporter to be shown to transport -aminobutyric acid (GABA). All previously identified bacterial GABA transporters are secondary carriers of the amino acid-polyamine-organocation (APC) superfamily. Also, transport by Bra_Rl does not appear to be stereospecific as D amino acids cause significant inhibition of uptake of L-glutamate and L-leucine. Unlike all other solutes tested, L-alanine uptake is not dependent on solute binding protein BraC_Rl. Therefore, a second, unidentified solute binding protein may interact with the BraDEFG_Rl membrane complex during L-alanine uptake. Overall, the data indicate that Bra_Rl is a general amino acid permease of the HAAT family. Furthermore, Bra_Rl has the broadest solute specificity of any characterized bacterial amino acid transporter.

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