Initial assembly steps of a translocase for folded proteins

Anne-Sophie Blümmel, Laura A. Haag, Ekaterina Eimer, Matthias Müller () and Julia Fröbel ()
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Anne-Sophie Blümmel: Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg
Laura A. Haag: Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg
Ekaterina Eimer: Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg
Matthias Müller: Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg
Julia Fröbel: Institute of Biochemistry and Molecular Biology, ZBMZ, University of Freiburg

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract The so-called Tat (twin-arginine translocation) system transports completely folded proteins across cellular membranes of archaea, prokaryotes and plant chloroplasts. Tat-directed proteins are distinguished by a conserved twin-arginine (RR-) motif in their signal sequences. Many Tat systems are based on the membrane proteins TatA, TatB and TatC, of which TatB and TatC are known to cooperate in binding RR-signal peptides and to form higher-order oligomeric structures. We have now elucidated the fine architecture of TatBC oligomers assembled to form closed intramembrane substrate-binding cavities. The identification of distinct homonymous and heteronymous contacts between TatB and TatC suggest that TatB monomers coalesce into dome-like TatB structures that are surrounded by outer rings of TatC monomers. We also show that these TatBC complexes are approached by TatA protomers through their N-termini, which thereby establish contacts with TatB and membrane-inserted RR-precursors.

Date: 2015
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DOI: 10.1038/ncomms8234

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