{"doi":"10.1111/j.1432-1033.1992.tb16636.x","title":"Role of the β subunit of casein kinase‐2 on the stability and specificity of the recombinant reconstituted holoenzyme","abstract":"<jats:p>Recombinant human α subunit from casein kinase‐2 (CK‐2) was subjected, either alone or in combination with recombinant human β subunit, to high temperature, tryptic digestion and urea treatment. In all three cases, it was shown that the presence of the β subunit could drastically reduce the loss of kinase activity, strongly suggesting a protective function for the β subunit. Assaying different peptides for specificity toward the recombinant α subunit and the recombinant reconstituted enzyme, showed that the presence of the β subunit could modify the specificity of the catalytic α subunit. Therefore, a dual function for the β subunit is proposed which confers both specificity and stability to the catalytic α subunit within the CK‐2 holoenzyme complex. The peptide DLEPDEELEDNPNQSDL, reproducing the highly acidic amino acid 55–71 segment of the human β subunit, counteracts the stimulatory effect of the β subunit on the α subunit activity and partially substitutes the β subunit in conferring thermal stability to the α subunit. No such effect is induced by the peptide MSSSEEVSW, reproducing the N‐terminal segment of the β subunit including the autophosphorylation site. It is suggested that the acidic domain of the β subunit, encompassing residues 55–71, plays a role in the interactions between the β and α subunits.</jats:p>","journal":"European Journal of Biochemistry","year":1992,"id":24859,"datarank":8.52731932590174,"base_score":5.087596335232384,"endowment":5.087596335232384,"self_citation_contribution":0.7631394502848576,"citation_network_contribution":7.764179875616882,"self_endowment_contribution":0.7631394502848576,"citer_contribution":7.764179875616882,"corpus_percentile":null,"corpus_rank":null,"citation_count":161,"citer_count":125,"citers_with_citation_signal":113,"citers_with_endowment":113,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":147921,"name":"Brigitte BOLDYREFF","orcid":null,"position":1,"is_corresponding":false},{"id":147922,"name":"Oriano MARIN","orcid":null,"position":2,"is_corresponding":false},{"id":147923,"name":"Lorenzo A. PINNA","orcid":null,"position":3,"is_corresponding":false},{"id":147924,"name":"Olaf‐Georg ISSINGER","orcid":null,"position":4,"is_corresponding":false},{"id":147920,"name":"Flavio MEGGIO","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":5.087596335232384,"endowment":5.087596335232384,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"1740140","pmcid":null,"openalex_id":"https://openalex.org/W1976532240","authors":[],"funders":[],"total_grants":0,"fwci":5.0329,"citation_percentile":0.9615063,"influential_citations":5,"citation_trend":[{"year":2012,"count":2},{"year":2013,"count":1},{"year":2014,"count":5},{"year":2015,"count":4},{"year":2016,"count":4},{"year":2017,"count":1},{"year":2018,"count":2},{"year":2019,"count":1},{"year":2020,"count":1},{"year":2021,"count":1},{"year":2022,"count":4},{"year":2023,"count":3},{"year":2024,"count":1},{"year":2025,"count":2}],"oa_status":"bronze","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1432-1033.1992.tb16636.x","host_type":"journal"},{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1432-1033.1992.tb16636.x","host_type":"BRONZE"},{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1432-1033.1992.tb16636.x","host_type":"publisher"},{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1992.tb16636.x","host_type":"publisher"},{"url":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1992.tb16636.x","host_type":"publisher"},{"url":"https://doi.org/10.1111/j.1432-1033.1992.tb16636.x","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/1740140","host_type":"repository"}],"fields_of_study":["Protein Hydrolysis and Bioactive Peptides","Enzyme Production and Characterization","Enzyme Structure and Function","Biology","Medicine","Chemistry","Amino Acid Sequence","Animals","Casein Kinases","Enzyme Stability","Hot Temperature","Kinetics","Liver","Macromolecular Substances","Magnesium","Molecular Sequence Data","Protein Kinases","Rats","Recombinant Proteins","Substrate Specificity","Urea"],"mesh_terms":["Amino Acid Sequence","Animals","Enzyme Stability","Hot Temperature","Kinetics","Liver","Magnesium","Molecular Sequence Data","Protein Kinases","Recombinant Proteins","Substrate Specificity","Urea","Macromolecular Substances","Casein Kinases","Rats"],"keywords":["Protein subunit","Gamma-aminobutyric acid receptor subunit alpha-1","Interleukin 10 receptor, alpha subunit","Recombinant DNA","Autophosphorylation","Specificity factor","G alpha subunit","Interleukin 5 receptor alpha subunit","Biochemistry","Gi alpha subunit","Molecular biology","BETA (programming language)","Casein kinase 2","Biology","Chemistry","Enzyme","Protein kinase A","Gene","Mitogen-activated protein kinase kinase"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-07T23:23:24.091271Z","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,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}