ArticleMolecular microbiology2012
Processing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- Length matters: Functional flip of the short TatA transmembrane helix.Biophysical journal · 2023Article
- Occurrence and potential mechanism of holin-mediated non-lytic protein translocation in bacteria.Microbial cell (Graz, Austria) · 2022Review
- C-terminal processing of GlyGly-CTERM containing proteins by rhombosortase in Vibrio cholerae.PLoS pathogens · 2018Article
- Article
- The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Molecular microbiology · 2015Article
- Identification of a Novel Dye-Decolorizing Peroxidase, EfeB, Translocated by a Twin-Arginine Translocation System in Streptococcus thermophilus CGMCC 7.179.Applied and environmental microbiology · 2015Article
- Initial assembly steps of a translocase for folded proteins.Nature communications · 2015Article
- Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site.Molecular microbiology · 2012Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The twin arginine transport (Tat) system transports folded proteins across the prokaryotic cytoplasmic membrane and the plant thylakoid membrane. In Escherichia coli three membrane proteins, TatA, TatB and TatC, are essential components of the machinery. TatA from Providencia stuartii is homologous to E. coli TatA but is synthesized as an inactive pre-protein with an N-terminal extension of eight amino acids. Removal of this extension by the rhomboid protease AarA is required to activate P. stuartii TatA. Here we show that P. stuartii TatA can functionally substitute for E. coli TatA provided that the E. coli homologue of AarA, GlpG, is present. The oligomerization state of the P. stuartii TatA pro-protein was compared with that of the proteolytically activated protein and with E. coli TatA. The pro-protein still formed small homo-oligomers but cannot form large TatBC-dependent assemblies. In the absence of TatB, E. coli TatA or the processed form of P. stuartii TatA form a complex with TatC. However, this complex is not observed with the pro-form of P. stuartii TatA. Taken together our results suggest that the P. stuartii TatA pro-protein is inactive because it is unable to interact with TatC and cannot form the large TatA complexes required for transport.
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