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
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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Nature communications 6 (2015), 7234, DOI 10.1038/ncomms8234, issn: 2041-1723
IN COPYRIGHT http://rightsstatements.org/page/InC/1.0 rs
- Klassifikation
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Biowissenschaften, Biologie
- Schlagwort
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Twin Arginine Translocation
- Ereignis
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Veröffentlichung
- (wo)
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Freiburg
- (wer)
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Universität
- (wann)
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2015
- Urheber
- Beteiligte Personen und Organisationen
- DOI
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10.1038/ncomms8234
- URN
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urn:nbn:de:bsz:25-freidok-127319
- Rechteinformation
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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15.08.2025, 07:21 MESZ
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Beteiligte
- Blümmel, Anne-Sophie
- Haag, Laura A.
- Eimer, Ekaterina
- Müller, Matthias
- Fröbel, Julia
- Institut für Biochemie und Molekularbiologie. Freiburg im Breisgau
- Spemann Graduate School of Biology and Medicine
- Albert-Ludwigs-Universität Freiburg. Fakultät für Biologie
- Albert-Ludwigs-Universität Freiburg
- Universität
Entstanden
- 2015