A larger TatBC complex associates with TatA clusters for transport of folded proteins across the bacterial cytoplasmic membrane.

Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE

Original Publication: London : Nature Publishing Group, copyright 2011-

Escherichia coli Proteins*/metabolism ; Escherichia coli Proteins*/genetics ; Escherichia coli Proteins*/chemistry ; Escherichia coli*/metabolism ; Escherichia coli*/genetics ; Membrane Transport Proteins*/metabolism ; Membrane Transport Proteins*/genetics ; Membrane Transport Proteins*/chemistry ; Cell Membrane*/metabolism ; Protein Transport*; Protein Folding ; Protein Binding ; Mutation

The twin-arginine translocation (Tat) system transports folded proteins across energized biological membranes in bacteria, plastids, and plant mitochondria. In Escherichia coli, the three membrane proteins TatA, TatB and TatC associate to enable Tat transport. While TatB and TatC together form complexes that bind Tat-dependently transported proteins, the TatA component is responsible for the permeabilization of the membrane during transport. With wild type Tat systems, the TatB- and TatC-containing Tat complexes TC1 and TC2 can be differentiated. Their TatA content has not been resolved, nor could they be assigned to any step of the translocation mechanism. It is therefore a key question of current Tat research to understand how TatA associates with Tat systems during transport. By analyzing affinity-purified Tat complexes with mutations in TatC that selectively enrich either TC1 or TC2, we now for the first time demonstrate that both Tat complexes associate with TatA, but the larger TC2 recruits significantly more TatA than the smaller TC1. Most TatA co-purified as multimeric clusters. Using site-specific photo cross-linking, we could detect TatA-TatC interactions only near TatC transmembrane helices 5 and 6. Substrate-binding did not change the interacting positions but affected the stability of the interaction, pointing to a substrate-induced conformational transition. Together, our findings indicate that TatA clusters associate with TatBC without being integrated into the complex by major rearrangements. The increased TatA affinity of the larger Tat complex TC2 suggests that functional assembly is advanced in this complex.
(© 2024. The Author(s).)

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BR 2285/8-1 Deutsche Forschungsgemeinschaft; BR 2285/8-1 Deutsche Forschungsgemeinschaft; BR 2285/8-1 Deutsche Forschungsgemeinschaft

0 (Escherichia coli Proteins)
0 (Membrane Transport Proteins)
0 (TatA protein, E coli)
0 (TatB protein, E coli)
0 (TatC protein, E coli)

Date Created: 20240614 Date Completed: 20240614 Latest Revision: 20240618

20240618

PMC11178869

10.1038/s41598-024-64547-x

38877109