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• W2048778654 startingPage "557" @default.
• W2048778654 abstract "Maximal repression by the CytR protein depends on the formation of nucleoprotein complexes in which CytR interacts with DNA and with cAMP-cAMP receptor protein (CRP). Here we demonstrate that CytR regulates transcription from deoP2 promoters in which the entire CytR recognition sequence has been eliminated. Furthermore, CytR proteins deleted for the DNA-binding domain repress deoP2 in vivo and interact with deoP2 in vitro in a strictly cAMP-CRP-dependent fashion. These experiments show that the site of action of CytR can be specified by protein-protein interactions to cAMP-CRP, whereas CytR-DNA interactions may primarily serve to stabilize the nucleo-protein complex. This type of specificity mechanism may represent a general concept in the recruitment of DNA-binding proteins in combinatorial regulatory systems." @default.
• W2048778654 created "2016-06-24" @default.
• W2048778654 creator A5074705819 @default.
• W2048778654 creator A5079298381 @default.
• W2048778654 date "1993-11-01" @default.
• W2048778654 modified "2023-10-13" @default.
• W2048778654 title "Protein-protein interactions in gene regulation: The cAMP-CRP complex sets the specificity of a second DNA-binding protein, the CytR repressor" @default.
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• W2048778654 doi "https://doi.org/10.1016/0092-8674(93)90389-8" @default.
• W2048778654 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8221894" @default.
• W2048778654 hasPublicationYear "1993" @default.
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