{"corpus_id":25416078,"paper_sha":"348780d9a3aa6fe8b5a10814ffcdacbe8dec355a","doi":"10.1074/JBC.M104855200","arxiv_id":null,"pmid":11527965,"pmcid":null,"mag_id":2005371789,"dblp_id":null,"acl_id":null,"title":"Multimerization of Phosphorylated and Non-phosphorylated ArcA Is Necessary for the Response Regulator Function of the Arc Two-component Signal Transduction System*","year":2001,"publication_date":"2001-11-02","venue":"Journal of Biological Chemistry","journal":{"name":"The Journal of Biological Chemistry","pages":"40873 - 40879","volume":"276"},"journal_issn":null,"journal_title":null,"publication_types":["JournalArticle"],"pubmed_pub_types":["Journal Article","Research Support, Non-U.S. Gov't"],"s2_fields_of_study":["Biology","Medicine","Chemistry"],"reference_count":26,"citation_count":98,"influential_citation_count":7,"is_open_access":true,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Bacterial Outer Membrane Proteins","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"isolation & purification","mj":false,"ui":"Q000302"},{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D001425"},{"d":"Base Sequence","mj":false,"ui":"D001483"},{"d":"Biopolymers","mj":false,"ui":"D001704"},{"d":"DNA Primers","mj":false,"ui":"D017931"},{"d":"Escherichia coli Proteins","mj":false,"ui":"D029968"},{"d":"Mutagenesis","mj":false,"ui":"D016296"},{"d":"Phosphorylation","mj":false,"ui":"D010766"},{"d":"Repressor Proteins","mj":true,"ui":"D012097"},{"d":"Signal Transduction","mj":true,"ui":"D015398"}],"chemicals":[{"n":"Bacterial Outer Membrane Proteins","ui":"D001425","reg":"0"},{"n":"Biopolymers","ui":"D001704","reg":"0"},{"n":"DNA Primers","ui":"D017931","reg":"0"},{"n":"Escherichia coli Proteins","ui":"D029968","reg":"0"},{"n":"Repressor Proteins","ui":"D012097","reg":"0"},{"n":"arcA protein, E coli","ui":"C041610","reg":"0"}],"comments_corrections":null,"source_flags":5,"s2_open_access_pdf_url":"http://www.jbc.org/article/S0021925820779342/pdf","s2_open_access_landing_url":"https://www.semanticscholar.org/paper/348780d9a3aa6fe8b5a10814ffcdacbe8dec355a","s2_open_access_license":"CCBY","s2_open_access_status":"HYBRID","pmc_open_access_pdf_url":null,"pmc_open_access_landing_url":null,"pmc_open_access_license":null,"pmc_open_access_status":null,"unpaywall_open_access_pdf_url":null,"unpaywall_open_access_landing_url":null,"unpaywall_open_access_license":null,"unpaywall_open_access_status":null,"abstract":"To adapt to anaerobic conditions,Escherichia coli operates the Arc two-component signal transduction system, consisting of a sensor kinase, ArcB, and a response regulator, ArcA. ArcA is converted to the active form, phosphorylated ArcA (ArcA-P), by ArcB-mediated phosphorylation. The active ArcA-P binds to the promoter regions of target genes, thereby regulating their transcriptional activities. The phosphoryl group of ArcA-P is unstable with a half-life of 30 min. However, we were able to inhibit the dephosphorylation for more than 12 h by the addition of EDTA; this allowed us to characterize ArcA-P. Gel-filtration and glycerol sedimentation experiments demonstrated that ArcA exists as a homo-dimer. ArcA phosphorylated by either ArcB or carbamyl phosphate multimerizes to form a tetramer of dimers; this multimer binds to the ArcA DNA binding site. Isoelectric focusing gel electrophoresis and nitrocellulose-filter binding analyses indicated that the ArcA multimer is composed of both ArcA-P and ArcA in a ratio, 1:1. The ArcA(D54E) mutant protein was unable to be phosphorylated by ArcB. This defect resulted in the inability of ArcA(D54E) to form a multimer or to bind to the ArcA DNA binding site. These results indicate that phosphorylation of ArcA induces multimerization prior to DNA binding, and the multimerization is a prerequisite for binding. Our results suggest a novel model that phosphorylation of ArcA by ArcB regulates multimerization of ArcA, which in turn functions as a response regulator.","claims":[{"public_id":"cl_de5cf873754a9cb5a919564c2e8bc8ad","status":"active","text":"ArcA exists as a homo-dimer, as demonstrated by gel-filtration and glycerol sedimentation experiments.","confidence":0.95,"contributors":[{"id":17,"public_id":"322360f1c1","public_label":"Killer Whale (322360f1c1)","roles":["extraction"],"url":"https://sah.borca.ai/u/322360f1c1"},{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["review"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_de5cf873754a9cb5a919564c2e8bc8ad"},{"public_id":"cl_9ed3449d13c8bde8cb99aef7331b9cc7","status":"active","text":"ArcA(D54E), unable to be phosphorylated by ArcB, cannot form a multimer or bind to the ArcA DNA binding 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