{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang Z"],"funding":["HHS | NIH | Office of Extramural Research, National Institutes of Health","NIAID NIH HHS"],"pagination":["e0343023"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10936212"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(3)"],"pubmed_abstract":["<i>Campylobacter jejuni</i> is a foodborne pathogen commonly found in the intestinal tracts of animals. This pathogen is a leading cause of gastroenteritis in humans. Besides its highly infectious nature, <i>C. jejuni</i> is increasingly resistant to a number of clinically administrated antibiotics. As a consequence, the Centers for Disease Control and Prevention has designated antibiotic-resistant <i>Campylobacter</i> as a serious antibiotic resistance threat in the United States. The <i>C. jejuni</i> CosR regulator is essential to the viability of this bacterium and is responsible for regulating the expression of a number of oxidative stress defense enzymes. Importantly, it also modulates the expression of the CmeABC multidrug efflux system, the most predominant and clinically important system in <i>C. jejuni</i> that mediates resistance to multiple antimicrobials. Here, we report structures of apo-CosR and CosR bound with a 21 bp DNA sequence located at the <i>cmeABC</i> promotor region using both single-particle cryo-electron microscopy and X-ray crystallography. These structures allow us to propose a novel mechanism for CosR regulation that involves a long-distance conformational coupling and rearrangement of the secondary structural elements of the regulator to bind target DNA.<h4>Importance</h4><i>Campylobacter jejuni</i> has emerged as an antibiotic-resistant threat worldwide. CosR is an essential regulator for this bacterium and is important for <i>Campylobacter</i> adaptation to various stresses. Here, we describe the structural basis of CosR binding to target DNA as determined by cryo-electron microscopy and X-ray crystallography. Since CosR is a potential target for intervention, our studies may facilitate the development of novel therapeutics to combat <i>C. jejuni</i> infection."],"journal":["mBio"],"pubmed_title":["Structural basis of DNA recognition of the <i>Campylobacter jejuni</i> CosR regulator."],"pmcid":["PMC10936212"],"funding_grant_id":["R01AI140669","R01 AI140669","R01AI145069, R01AI140669","R01 AI145069"],"pubmed_authors":["Dai L","Zhang Z","Pang J","Yan Y","Yu EW","Zhang Q"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis of DNA recognition of the <i>Campylobacter jejuni</i> CosR regulator.","description":"<i>Campylobacter jejuni</i> is a foodborne pathogen commonly found in the intestinal tracts of animals. This pathogen is a leading cause of gastroenteritis in humans. Besides its highly infectious nature, <i>C. jejuni</i> is increasingly resistant to a number of clinically administrated antibiotics. As a consequence, the Centers for Disease Control and Prevention has designated antibiotic-resistant <i>Campylobacter</i> as a serious antibiotic resistance threat in the United States. The <i>C. jejuni</i> CosR regulator is essential to the viability of this bacterium and is responsible for regulating the expression of a number of oxidative stress defense enzymes. Importantly, it also modulates the expression of the CmeABC multidrug efflux system, the most predominant and clinically important system in <i>C. jejuni</i> that mediates resistance to multiple antimicrobials. Here, we report structures of apo-CosR and CosR bound with a 21 bp DNA sequence located at the <i>cmeABC</i> promotor region using both single-particle cryo-electron microscopy and X-ray crystallography. These structures allow us to propose a novel mechanism for CosR regulation that involves a long-distance conformational coupling and rearrangement of the secondary structural elements of the regulator to bind target DNA.<h4>Importance</h4><i>Campylobacter jejuni</i> has emerged as an antibiotic-resistant threat worldwide. CosR is an essential regulator for this bacterium and is important for <i>Campylobacter</i> adaptation to various stresses. Here, we describe the structural basis of CosR binding to target DNA as determined by cryo-electron microscopy and X-ray crystallography. Since CosR is a potential target for intervention, our studies may facilitate the development of novel therapeutics to combat <i>C. jejuni</i> infection.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-06-27T03:10:11.098Z","creation":"2026-06-27T03:05:15.952Z"},"accession":"S-EPMC10936212","cross_references":{"pubmed":["38323832"],"doi":["10.1128/mbio.03430-23"]}}