Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870532 | FEBS Letters | 2015 | 6 Pages |
Abstract
Cyclic AMP receptor protein (CRP), the global transcription regulator in prokaryotes, is active only as a cAMP-CRP complex. Binding of cAMP changes the conformation of CRP, transforming it from a transcriptionally 'inactive' to an 'active' molecule. These conformers are also characterized by distinct biochemical properties including the ability to form an S-S crosslink between the C178 residues of its two monomeric subunits. We studied a CRP variant (CRPcl), in which the subunits are crosslinked. We demonstrate that CRPcl can activate transcription even in the absence of cAMP. Implications of these results for the crystallographically-determined structure of cAMP-CRP are discussed.
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Authors
Abinit Saha, Jayanta Mukhopadhyay, Ajit Bikram Datta, Pradeep Parrack,