{"doi":"10.1038/ncomms2308","title":"Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB","abstract":null,"journal":"Nature Communications","year":2012,"id":658430,"datarank":0.6238324625039509,"base_score":4.1588830833596715,"endowment":4.1588830833596715,"self_citation_contribution":0.6238324625039509,"citation_network_contribution":0.0,"self_endowment_contribution":0.6238324625039509,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":63,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1718819,"name":"Patrick Rose","orcid":null,"position":1,"is_corresponding":false},{"id":1718820,"name":"Frank Lausberg","orcid":null,"position":2,"is_corresponding":false},{"id":1718821,"name":"Anne-Sophie Blümmel","orcid":null,"position":3,"is_corresponding":false},{"id":1718822,"name":"Roland Freudl","orcid":null,"position":4,"is_corresponding":false},{"id":1264724,"name":"Matthias Müller","orcid":"0000-0002-8480-0253","position":5,"is_corresponding":false},{"id":1718818,"name":"Julia Fröbel","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Transmembrane insertion of twin-arginine signal peptides is driven by TatC and regulated by TatB","abstract":"The twin-arginine translocation (Tat) pathway of bacteria and plant chloroplasts mediates the transmembrane transport of folded proteins, which harbour signal sequences with a conserved twin-arginine motif. Many Tat translocases comprise the three membrane proteins TatA, TatB and TatC. TatC was previously shown to be involved in recognizing twin-arginine signal peptides. Here we show that beyond recognition, TatC mediates the transmembrane insertion of a twin-arginine signal sequence, thereby translocating the signal sequence cleavage site across the bilayer. In the absence of TatB, this can lead to the removal of the signal sequence even from a translocation-incompetent substrate. Hence interaction of twin-arginine signal peptides with TatB counteracts their premature cleavage uncoupled from translocation. This capacity of TatB is not shared by the homologous TatA protein. Collectively our results suggest that TatC is an insertase for twin-arginine signal peptides and that translocation-proficient signal sequence recognition requires the concerted action of TatC and TatB.","is_dataset_classified":null,"base_score":4.1588830833596715,"endowment":4.1588830833596715,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23250441","pmcid":"PMC3538955","openalex_id":"https://openalex.org/W2109802625","authors":[],"funders":[],"total_grants":0,"fwci":10.1124,"citation_percentile":0.98226072,"influential_citations":5,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":8},{"year":2014,"count":11},{"year":2015,"count":7},{"year":2016,"count":4},{"year":2017,"count":3},{"year":2018,"count":7},{"year":2019,"count":5},{"year":2020,"count":2},{"year":2021,"count":4},{"year":2022,"count":5},{"year":2023,"count":1},{"year":2024,"count":2},{"year":2025,"count":3}],"oa_status":"hybrid","license":"cc-by-nc-nd","oa_locations":[{"url":"https://www.nature.com/articles/ncomms2308.pdf","host_type":"journal"},{"url":"https://www.nature.com/articles/ncomms2308.pdf","host_type":"HYBRID"},{"url":"https://www.nature.com/articles/ncomms2308.pdf","host_type":"publisher"},{"url":"http://www.nature.com/articles/ncomms2308","host_type":"publisher"},{"url":"http://www.nature.com/articles/ncomms2308.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1038/ncomms2308","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/23250441","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3538955","host_type":"repository"},{"url":"https://www.nature.com/articles/ncomms2308","host_type":"repository"},{"url":"http://juser.fz-juelich.de/search?p=id:%22FZJ-2013-00404%22","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC3538955","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC3538955?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Legume Nitrogen Fixing Symbiosis","Bacterial Genetics and Biotechnology","Photosynthetic Processes and Mechanisms","Medicine","Biology","Environmental Science","Escherichia coli","Escherichia coli Proteins","Membrane Transport Proteins","Protein Sorting Signals"],"mesh_terms":["Escherichia coli","Protein Sorting Signals","Membrane Transport Proteins","Escherichia coli Proteins"],"keywords":["Twin-arginine translocation pathway","TATB","Transmembrane protein","Signal peptide","SIGNAL (programming language)","Arginine","Transmembrane domain","Cell biology","Biophysics","Membrane transport protein","Chemistry","Membrane","Membrane protein","Biology","Biochemistry","Peptide sequence","Computer science","Amino acid"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life below water"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T04:12:35.985277Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}