Initial assembly steps of a translocase for folded proteins

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

Standort
Deutsche Nationalbibliothek Frankfurt am Main
Umfang
Online-Ressource
Sprache
Englisch
Anmerkungen
Nature communications 6 (2015), 7234, DOI 10.1038/ncomms8234, issn: 2041-1723
IN COPYRIGHT http://rightsstatements.org/page/InC/1.0 rs

Klassifikation
Biowissenschaften, Biologie
Schlagwort
Twin Arginine Translocation

Ereignis
Veröffentlichung
(wo)
Freiburg
(wer)
Universität
(wann)
2015
Urheber
Beteiligte Personen und Organisationen

DOI
10.1038/ncomms8234
URN
urn:nbn:de:bsz:25-freidok-127319
Rechteinformation
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Letzte Aktualisierung
15.08.2025, 07:21 MESZ

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