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Peros M, Steitz T: DNA looping and Lac repressor CAP interaction. Science 1996, 274:1929-1930. The authors present an experiment which excludes the possibility that the Lac repressor and CAP can bind together when their sites are 20.5 bp apart as in the lac promoter region. This had been postulated by Lewis et al, 1996 [8••] and put as model on the cover of Science.
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Fried MG, Hudson M: DNA looping and Lac repressor CAP interaction. Science 1996, 274:1931-1932. The authors present an experiment which indicates that Lac repressor and CAP may form a ternary loop complex on a piece of DNA containing the lac promoter region. Yet, the binding of Lac repressor to O3 is abnormal. Is it really O3?
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Lewis M: DNA looping and Lac repressor CAP interaction. Science 1996, 274:1931-1932. The author defends his model of a ternary loop complex between the CAP-Lac repressor and the O1-O3 lac operators. Who is right? Who is wrong?
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Suckow J, Markiewicz P, Kleina LG, Miller J, Kisters-Woike B, Müller-Hill B: Genetic studies of the lac repressor XV: 4000 single amino acid substitutions and the analysis of the resulting phenotypes on the basis of protein structure. J Mol Biol 1996, 261:509-523. At last, Jeffrey Miller's 4000 point mutations of the Lac repressor are presented. The phenotypes of the mutants are discussed in the light of the recent X-ray and NMR structures.
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Aki T, Choy HE, Adhya S: Histone-like protein HU as a specific transcriptional regulator: co-factor role in repression of gal transcription by Gal repressor. Genes to Cells 1996, 1:179-188 Their inability to detect loops made by Gal repressor between the two gal operators in vitro led the authors to conclude that an auxiliary protein must exist. They looked for it and found it. The amino-terminal sequence revealed that it was HU.
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Aki T, Adhya S: Repressor induced site-specific binding of HU for transcriptional regulation. EMBO J 1997, 16:3666-3674. The authors continue their analysis of HU as an auxiliary protein in loop formation of Gal repressor dimers. Their detailed in vitro experiments are most informative.
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Hsieh M, Brenowitz M: Comparison of the DNA association kinetics of the lac repressor tetramer, its dimeric mutant Lacladi, and the native dimeric gaf repressor. J Biol Chem 1997, 272:22092-22096.
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Kristensen H-H, Valentin-Hansen PV, Søgaard-Andersen L: CytR/cAMP-CRP nucleoprotein formation in E. coli: the Cyt repressor binds its operator as a stable dimer in a ternary complex with cAMP-CRP. J Mol Biol 1996, 260:113-119.
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Rasmussen PB, Holst B, Valentin-Hansen P: Dual function regulators: the cAMP receptor protein and the CytR regulator can act either to repress or to activate transcription depending on the context. Proc Natl Acad Sci USA 1996, 93:10151-10155. The authors present a clever experiment which documents that the Cyt repressor can work together with CAP as a co-activator. In the proper construct CytR may tighten CAP binding to a weak (L8) CAP site by binding to the CAP subunit which does not interact with RNA polymerase.
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Perini LT, Doherty EA, Werner E, Senear DF: Multiple specific CytR binding sites at the Escherichia coli deoP2 promoter mediate both cooperative and competitive interactions between CytR and cAMP receptor protein. J Biol Chem 1996, 52:33242-33255.
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Pedersen H, Valentin Hansen P: Protein induced fit: the CRP activator protein changes sequence-specific DNA recognition by the CytR repressor, a highly flexible Lacl member. EMBO J 1997, 16:2108-2118. The authors present evidence that the Cyt repressor binds specifically to DNA in a different manner when it is alone or either when it is held by CAP. Its hinge helix must be flexible to allow drastically different spacing.
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Kallipolitis BH, Nørregaard-Madsen M, Valentin-Hansen P; Protein-protein communication: structural model of the repression complex formed by CytR and the global regulator CRP. Cell 1997, 89:1101-1109. CAP mutants are known which do not help Cyt represser to repress. The authors isolated Cyt repressor mutants which overcome (suppress) the defect in these CAP mutants. From their data, they propose structural models of the Cyt repressor-CAP-DNA complexes operating in vivo.
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Kristensen H-H, Valentin-Hansen P, Søgaard-Andersen L: Design of a CytR regulated, cAMP-CRP dependent classII promoter in Escherichia coli: RNA polymerase-promoter interactions modulate the efficiency of CytR repression. J Mol Biol 1997, 266:866-876.
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Brikun I, Suziedelis K, Stemmann O, Zhang R, Alikhanian L, Linkova E, Mironov A, Berg DE: Analysis of CRP-CytR interactions at the Escherichia coli upd promoter. J Bacteriol 1996, 178:1614-1622.
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Tyrrell R, Verschueren KHG, Dodsen EJ, Murshudov GN, Addy C, Wilkinson AJ: The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement Structure 1997, 5:1017-1032. A striking example that a good invention, here the repressor core, can be used in different ways. The cores of the Lac repressor and of CysB (an activator) have similar three dimensional structures. Two monomers assemble in a parallel manner in the Lac repressor and in an antiparallel manner in CysB, when they form dimers.
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Structure
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