ArticleJournal of bacteriology2002
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.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed, 100 citations in OpenAlex.
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- Diauxie and co-utilization of carbon sources can coexist during bacterial growth in nutritionally complex environments.Nature communications · 2020Article
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- Genomic Insights Into the Lifestyles of Thaumarchaeota Inside Sponges.Frontiers in microbiology · 2020Article
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- Characterization of a thaumarchaeal symbiont that drives incomplete nitrification in the tropical sponge Ianthella basta.Environmental microbiology · 2019Article
- Transcriptomic analysis of Rhizobium leguminosarum bacteroids in determinate and indeterminate nodules.Microbial genomics · 2019Article
- Complete genome of RhizobiumStandards in genomic sciences · 2018Article
- How fish eggs are preadapted for the evolution of matrotrophy.Proceedings. Biological sciences · 2017Article
- Integrated metabolism in sponge-microbe symbiosis revealed by genome-centered metatranscriptomics.The ISME journal · 2017Article
- Glutathione affects the transport activity of Rhizobium leguminosarum 3841 and is essential for efficient nodulation.FEMS microbiology letters · 2017Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
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 alpha-amino acids. Consistent with this, Bra(Rl) is the first ABC transporter to be shown to transport gamma-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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