WebNov 9, 2002 · The Escherichia coli biotin repressor, an allosteric transcriptional regulator, is activated for binding to the biotin operator by the small molecule biotinyl-5‘-AMP. Results of combined thermodynamic, kinetic, and structural studies of the protein have revealed that corepressor binding results in disorder to order transitions in the protein monomer that … WebDec 25, 1982 · A bifunctional protein. Definitive evidence is presented for the bifunctional …
Corepressor-induced organization and assembly of the …
WebEnzymatic Biotinylation: BirA. Ligation of biotin to a protein is a specific post-translational … WebAug 1, 2008 · The biotin repressor is an allosterically regulated, site-specific DNA-binding protein. Binding of the small ligand bio-5′-AMP activates repressor dimerization, which is a prerequisite to DNA binding.Multiple disorder-to-order transitions, some of which are known to be important for the functional allosteric response, occur in the vicinity of the ligand … lycee foot internat
Evidence for Interdomain Interaction in the Escherichia coli Repressor …
WebWe also demonstrate that the S. aureus BirA protein is a transcriptional repressor of … WebNov 11, 1991 · Proteins most abundant in S-phase cells were stress associated and transporters plus transferases in agreement with the general phenomenon that binding protein-dependent systems are induced under nutrient limitation as part of hunger response. ... The Escherichia coli biotin repressor is a member of the “winged helix-turn-helix” … WebFeb 2, 2005 · The Escherichia coli biotin repressor is an allosteric DNA binding protein and is activated by the small molecule bio-5‘-AMP. Binding of this small molecule promotes transcription repression complex assembly between the repressor and the biotin operator of the biotin biosynthetic operon. kingstar technology inc