{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(10)"],"submitter":["Singh R"],"pubmed_abstract":["HapR has been given the status of a high cell density master regulatory protein in Vibrio cholerae. Though many facts are known regarding its structural and functional aspects, much still can be learnt from natural variants of the wild type protein. This work aims at investigating the nature of functional inertness of a HapR natural variant harboring a substitution of a conserved glutamate residue at position 117 which participates in forming a salt bridge by lysine (HapRV2G-E(117)K). Experimental evidence presented here reveals the inability of this variant to interact with various cognate promoters by in vitro gel shift assay. Furthermore, the elution profiles of HapRV2G-E(117)K protein along with the wild type functional HapRV2G in size-exclusion chromatography as well as circular dichr"],"journal":["PloS one"],"pagination":["e76033"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3796514"],"repository":["biostudies-literature"],"pubmed_title":["Substitution of glutamate residue by lysine in the dimerization domain affects DNA binding ability of HapR by inducing structural deformity in the DNA binding domain."],"pmcid":["PMC3796514"],"pubmed_authors":["Peddada N","Rathore YS","Ashish","Singh R","Raychaudhuri S","Singh NS"],"additional_accession":[]},"is_claimable":false,"name":"Substitution of glutamate residue by lysine in the dimerization domain affects DNA binding ability of HapR by inducing structural deformity in the DNA binding domain.","description":"HapR has been given the status of a high cell density master regulatory protein in Vibrio cholerae. Though many facts are known regarding its structural and functional aspects, much still can be learnt from natural variants of the wild type protein. This work aims at investigating the nature of functional inertness of a HapR natural variant harboring a substitution of a conserved glutamate residue at position 117 which participates in forming a salt bridge by lysine (HapRV2G-E(117)K). Experimental evidence presented here reveals the inability of this variant to interact with various cognate promoters by in vitro gel shift assay. Furthermore, the elution profiles of HapRV2G-E(117)K protein along with the wild type functional HapRV2G in size-exclusion chromatography as well as circular dichr","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013","modification":"2025-04-04T11:09:46.174Z","creation":"2019-03-26T23:16:34Z"},"accession":"S-EPMC3796514","cross_references":{"pubmed":["24155884"],"doi":["10.1371/journal.pone.0076033"]}}