DNA-binding properties of a lac repressor mutant incapable of forming tetramers.
作者： A Pickar , M Brenowitz , E Jamison , N Mandal , S Adhya
DOI: 10.1016/S0021-9258(17)35313-9
关键词:
摘要: The interaction of proteins bound to sites widely separated on the genome is a recurrent motif in both prokaryotic and eukaryotic regulatory systems. Lac repressor mediates formation "DNA loops" by simultaneous single protein tetramer with two DNA-binding sites. properties mutant (LacIadi) deficient association dimers tetramers was investigated. results quantitative footprint gel mobility-shift titrations suggest that wild-type (LacI+) binds cooperatively operator 11 helical turns linear DNA restriction fragment "looped complex." LacIadi this two-site non-cooperatively without looped complex. These demonstrate dimer-tetramer LacI+ directly responsible for its cooperative binding ability mediate Iadi mutation disrupts monomer-dimer as well eliminating equilibria while affinity site unchanged relative protein. are functionally unlinked. similarity Gal repressor, believed function mediating complex, discussed.
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