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http://purl.uniprot.org/citations/31133615http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31133615http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31133615http://www.w3.org/2000/01/rdf-schema#comment"Inorganic polyphosphates (polyPs) are linear polymers of orthophosphate units linked by phosphoanhydride bonds. Here, we report that bacterial, archaeal, and eukaryotic conserved histidine α-helical (CHAD) domains are specific polyP-binding modules. Crystal structures reveal that CHAD domains are formed by two four-helix bundles, giving rise to a central pore surrounded by conserved basic surface patches. Different CHAD domains bind polyPs with dissociation constants ranging from the nano-to mid-micromolar range, but not nucleic acids. A CHAD-polyP complex structure reveals the phosphate polymer binding across the central pore and along the two basic patches. Mutational analysis of CHAD-polyP interface residues validates the complex structure. The presence of a CHAD domain in the polyPase ygiF enhances its enzymatic activity. The only known CHAD protein from the plant Ricinus communis localizes to the nucleus/nucleolus when expressed in Arabidopsis and tobacco, suggesting that plants may harbor polyPs in these compartments. We propose that CHAD domains may be used to engineer the properties of polyP-metabolizing enzymes and to specifically localize polyP stores in eukaryotic cells and tissues."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.org/dc/terms/identifier"doi:10.26508/lsa.201900385"xsd:string
http://purl.uniprot.org/citations/31133615http://purl.org/dc/terms/identifier"doi:10.26508/lsa.201900385"xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/author"Zhu J."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/author"Zhu J."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/author"Hothorn M."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/author"Hothorn M."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/author"Hohmann U."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/author"Hohmann U."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/author"Lorenzo-Orts L."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/author"Lorenzo-Orts L."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/name"Life. Sci Alliance"xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/name"Life Sci Alliance"xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/pages"e201900385"xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/pages"e201900385"xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/title"Molecular characterization of CHAD domains as inorganic polyphosphate-binding modules. ."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/title"Molecular characterization of CHAD domains as inorganic polyphosphate-binding modules."xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/volume"2"xsd:string
http://purl.uniprot.org/citations/31133615http://purl.uniprot.org/core/volume"2"xsd:string
http://purl.uniprot.org/citations/31133615http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31133615
http://purl.uniprot.org/citations/31133615http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31133615