The Tat-dependent protein translocation pathway

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dc.identifier.uri http://dx.doi.org/10.15488/3161
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/3191
dc.contributor.author Hou, Bo
dc.contributor.author Brüser, Thomas
dc.date.accessioned 2018-04-19T07:53:07Z
dc.date.available 2018-04-19T07:53:07Z
dc.date.issued 2011
dc.identifier.citation Hou, B.; Brüser, T.: The Tat-dependent protein translocation pathway. In: Biomolecular Concepts 2 (2011), Nr. 6, S. 507-523. DOI: https://doi.org/10.1515/BMC.2011.040
dc.description.abstract The twin-arginine translocation (Tat) pathway is found in bacteria, archaea, and plant chloroplasts, where it is dedicated to the transmembrane transport of fully folded proteins. These proteins contain N-terminal signal peptides with a specific Tat-system binding motif that is recognized by the transport machinery. In contrast to other protein transport systems, the Tat system consists of multiple copies of only two or three usually small (∼8-30 kDa) membrane proteins that oligomerize to two large complexes that transiently interact during translocation. Only one of these complexes includes a polytopic membrane protein, TatC. The other complex consists of TatA. Tat systems of plants, proteobacteria, and several other phyla contain a third component, TatB. TatB is evolutionarily and structurally related to TatA and usually forms tight complexes with TatC. Minimal two-component Tat systems lacking TatB are found in many bacterial and archaeal phyla. They consist of a 'bifunctional' TatA that also covers TatB functionalities, and a TatC. Recent insights into the structure and interactions of the Tat proteins have various important implications. © 2011 by Walter de Gruyter Berlin Boston 2011. eng
dc.language.iso eng
dc.publisher Berlin : De Gruyter
dc.relation.ispartofseries Biomolecular Concepts 2 (2011), Nr. 6
dc.rights Es gilt deutsches Urheberrecht. Das Dokument darf zum eigenen Gebrauch kostenfrei genutzt, aber nicht im Internet bereitgestellt oder an Außenstehende weitergegeben werden. Dieser Beitrag ist aufgrund einer (DFG-geförderten) Allianz- bzw. Nationallizenz frei zugänglich.
dc.subject protein folding eng
dc.subject protein transport eng
dc.subject redox protein biogenesis eng
dc.subject twin-arginine translocation eng
dc.subject Archaea eng
dc.subject Bacteria (microorganisms) eng
dc.subject Proteobacteria eng
dc.subject.ddc 500 | Naturwissenschaften ger
dc.title The Tat-dependent protein translocation pathway
dc.type article
dc.type Text
dc.relation.issn 1868-5021
dc.relation.doi https://doi.org/10.1515/BMC.2011.040
dc.bibliographicCitation.issue 6
dc.bibliographicCitation.volume 2
dc.bibliographicCitation.firstPage 507
dc.bibliographicCitation.lastPage 523
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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