The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter

Mulligan C; Geertsma ER; Severi EKelly DJPoolman BThomas GH

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The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter

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Substrate-binding protein-dependent secondary transporters are widespread in prokaryotes and are represented most frequently by members of the tripartite ATP-independent periplasmic (TRAP) transporter family. Here, we report the membrane reconstitution of a TRAP transporter, the sialic acid-specific SiaPQM system from Haemophilus influenzae, and elucidate its mechanism of energy coupling. Uptake of sialic acid via membrane-reconstituted SiaQM depends on the presence of the sialic acid-binding protein, SiaP, and is driven by the electrochemical sodium gradient. The interaction between SiaP and SiaQM is specific as transport is not reconstituted using the orthologous sialic acid-binding protein VC1779. Importantly, the binding protein also confers directionality on the transporter, and reversal of sialic acid transport from import to export is only possible in the presence of an excess of unliganded SiaP.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2009年第6期|1778-1783|共6页
作者
Mulligan C; Geertsma ER; Severi EKelly DJPoolman BThomas GH;
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作者单位

Univ York, Dept Biol, Area 10, York YO10 5YW, N Yorkshire, England.;

Univ Groningen, Dept Biochem, Groningen Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands.;

Univ Sheffield, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England.;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
sialic acid; SiaPQM; tripartite ATP-independent periplasmic transporter; Haemophilus influenzae; receptor-dependent translocation;

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The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter

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