A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli

Download statistics - Document (COUNTER):

Geise, H.; Heidrich, E.S.; Nikolin, C.S.; Mehner-Breitfeld, D.; Brüser, T.: A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli. In: Frontiers in Microbiology 10 (2019), 1482. DOI: https://doi.org/10.3389/fmicb.2019.01482

Repository version

To cite the version in the repository, please use this identifier: https://doi.org/10.15488/5218

Selected time period:

year: 
month: 

Sum total of downloads: 9




Thumbnail
Abstract: 
The twin-arginine translocation (Tat) system transports folded proteins across membranes of prokaryotes, plant plastids, and some mitochondria. According to blue-native polyacrylamide gel electrophoresis after solubilization with digitonin, distinct interactions between the components TatA, TatB, and TatC result in two major TatBC-containing complexes in Escherichia coli that can bind protein substrates. We now report the first detection of a TatABC complex that likely represents the state at which transport occurs. This complex was initially found when the photo cross-linking amino acid p-benzoyl-L-phenylalanine (Bpa) was introduced at position I50 on the periplasmic side of the first trans-membrane domain of TatC. Cross-linking of TatCI50Bpa resulted in TatC-TatC-cross-links, indicating a close proximity to neighboring TatC in the complex. However, the new complex was not caused by cross-links but rather by non-covalent side chain interactions, as it was also detectable without UV-cross-linking or with an I50Y exchange. The new complex did not contain any detectable substrate. It was slightly upshifted relative to previously reported substrate-containing TatABC complexes. In the absence of TatA, an inactive TatBCI50Bpa complex was formed of the size of wild-type substrate-containing TatABC complexes, suggesting that TatB occupies TatA-binding sites at TatCI50Bpa. When substrate binding was abolished by point mutations, this TatBCI50Bpa complex shifted analogously to active TatABCI50Bpa complexes, indicating that a defect substrate-binding site further enhances TatB association to TatA-binding sites. Only TatA could shift the complex with an intact substrate-binding site, which explains the TatA requirement for substrate transport by TatABC systems.
License of this version: CC BY 4.0
Document Type: article
Publishing status: publishedVersion
Issue Date: 2019
Appears in Collections:Naturwissenschaftliche Fakultät

distribution of downloads over the selected time period:

downloads by country:

pos. country downloads
total perc.
1 image of flag of Germany Germany 9 100.00%

Further download figures and rankings:


Hinweis

Zur Erhebung der Downloadstatistiken kommen entsprechend dem „COUNTER Code of Practice for e-Resources“ international anerkannte Regeln und Normen zur Anwendung. COUNTER ist eine internationale Non-Profit-Organisation, in der Bibliotheksverbände, Datenbankanbieter und Verlage gemeinsam an Standards zur Erhebung, Speicherung und Verarbeitung von Nutzungsdaten elektronischer Ressourcen arbeiten, welche so Objektivität und Vergleichbarkeit gewährleisten sollen. Es werden hierbei ausschließlich Zugriffe auf die entsprechenden Volltexte ausgewertet, keine Aufrufe der Website an sich.

Search the repository


Browse