{"doi":"10.1126/sciadv.aed8943","title":"Dimer asymmetry in signaling of blue light sensor histidine kinases","abstract":"<jats:p>\n                    Photoreceptor sensory histidine kinases (SHKs) couple light absorption to conformational changes regulating two-component signaling. Despite their importance and widespread use in optogenetics, the underlying structural signaling mechanisms remain poorly understood. Here, we engineered dimeric SHKs based on\n                    <jats:italic toggle=\"yes\">Pseudomonas putida</jats:italic>\n                    short light-oxygen-voltage (LOV) proteins, determined their crystal structures, and investigated their signaling mechanisms. Regardless of illumination, the structures adopted a light-state like LOV-LOV dimer with symmetric/straight kinase modules. In contrast, small-angle x-ray scattering together with functional assays revealed pronounced light-dependent rearrangements in solution and allowed the assignment of the kinase-ON dark state to an asymmetric/kinked conformation, whereas the light state adopts a symmetric/straight structure. Comparative analyses of natural and engineered SHKs identified conserved motifs linking light-induced LOV domain rotation to kinase activity. The findings highlight the central role of dimer asymmetry and flexibility in SHK signaling, thereby not least informing the engineering of new light-responsive signaling systems.\n                  </jats:p>","journal":"Science Advances","year":2026,"id":671744,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"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":1421440,"name":"Andreas Stadler","orcid":"0000-0003-2272-5232","position":1,"is_corresponding":false},{"id":1755008,"name":"Stefanie S.M. Meier","orcid":"0009-0002-6028-5223","position":2,"is_corresponding":false},{"id":1755009,"name":"Karl-Erich Jaeger","orcid":"0000-0002-6036-0708","position":3,"is_corresponding":false},{"id":1755010,"name":"Andreas Möglich","orcid":"0000-0002-7382-2772","position":4,"is_corresponding":false},{"id":1755011,"name":"Ulrich Krauss","orcid":"0000-0003-2219-7388","position":5,"is_corresponding":false},{"id":1342840,"name":"Renu Batra","orcid":"0000-0002-8597-4335","position":6,"is_corresponding":false},{"id":1755007,"name":"Vladimir Arinkin","orcid":"0000-0002-9210-9366","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Dimer asymmetry in signaling of blue light sensor histidine kinases","abstract":"<jats:p>\n                    Photoreceptor sensory histidine kinases (SHKs) couple light absorption to conformational changes regulating two-component signaling. Despite their importance and widespread use in optogenetics, the underlying structural signaling mechanisms remain poorly understood. Here, we engineered dimeric SHKs based on\n                    <jats:italic toggle=\"yes\">Pseudomonas putida</jats:italic>\n                    short light-oxygen-voltage (LOV) proteins, determined their crystal structures, and investigated their signaling mechanisms. Regardless of illumination, the structures adopted a light-state like LOV-LOV dimer with symmetric/straight kinase modules. In contrast, small-angle x-ray scattering together with functional assays revealed pronounced light-dependent rearrangements in solution and allowed the assignment of the kinase-ON dark state to an asymmetric/kinked conformation, whereas the light state adopts a symmetric/straight structure. Comparative analyses of natural and engineered SHKs identified conserved motifs linking light-induced LOV domain rotation to kinase activity. The findings highlight the central role of dimer asymmetry and flexibility in SHK signaling, thereby not least informing the engineering of new light-responsive signaling systems.\n                  </jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"42384803","pmcid":null,"openalex_id":"https://openalex.org/W4415559102","authors":[],"funders":[{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"MO2192/4-2","title":null},{"funder_name":"German Federal Ministry of Education and Research","grant_id":"Project OptoSys, FKZ 031A16 and FKZ031A167B","title":null}],"total_grants":2,"fwci":0.0,"citation_percentile":0.00283876,"influential_citations":0,"citation_trend":[],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://www.science.org/doi/pdf/10.1126/sciadv.aed8943?download=true","host_type":"journal"},{"url":"https://www.science.org/doi/pdf/10.1126/sciadv.aed8943?download=true","host_type":"publisher"},{"url":"https://www.science.org/doi/pdf/10.1126/sciadv.aed8943","host_type":"publisher"},{"url":"https://doi.org/10.1126/sciadv.aed8943","host_type":"journal"},{"url":"https://doi.org/10.1101/2025.10.24.684451","host_type":"repository"},{"url":"https://pubmed.ncbi.nlm.nih.gov/42384803","host_type":"repository"}],"fields_of_study":["Light effects on plants","Photoreceptor and optogenetics research","bioluminescence and chemiluminescence research","Histidine Kinase","Pseudomonas putida","Signal Transduction","Blue Light","Protein Multimerization","Models, Molecular","Bacterial Proteins","Protein Conformation","Crystallography, X-Ray","Light"],"mesh_terms":["Histidine Kinase","Blue Light","Bacterial Proteins","Light","Models, Molecular","Protein Conformation","Signal Transduction","Pseudomonas putida","Crystallography, X-Ray","Protein Multimerization"],"keywords":["Dimer","Histidine kinase","Kinase","Histidine","Protein kinase domain","Signal transduction","Flexibility (engineering)","Protein subunit","Protein structure"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T04:17:23.697418Z","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":[]}