The gene encoding the periplasmic cyclophilin homologue, PPIase A, in 
Escherichia coli, is expressed from four promoters, three of which are 
activated by the cAMP-CRP complex and negatively regulated by the CytR repressor

Norregaard-Madsen, M; Mygind, B; Pedersen, R; Valentin-Hansen, P; Sogaard-Andersen, Lotte

doi:10.1111/j.1365-2958.1994.tb01333.x

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The gene encoding the periplasmic cyclophilin homologue, PPIase A, in Escherichia coli, is expressed from four promoters, three of which are activated by the cAMP-CRP complex and negatively regulated by the CytR repressor

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Citation

Norregaard-Madsen, M., Mygind, B., Pedersen, R., Valentin-Hansen, P., & Sogaard-Andersen, L. (1994). The gene encoding the periplasmic cyclophilin homologue, PPIase A, in Escherichia coli, is expressed from four promoters, three of which are activated by the cAMP-CRP complex and negatively regulated by the CytR repressor. MOLECULAR MICROBIOLOGY, 14(5), 989-997. doi:10.1111/j.1365-2958.1994.tb01333.x.

Cite as: https://hdl.handle.net/21.11116/0000-0008-D66B-F

Abstract

The rot gene in Escherichia coli encodes PPlase A, a periplasmic peptidyl-prolyl cis-trans isomerase with homology to the cyclophilin family of proteins. Here it is demonstrated that rot is expressed in a complex manner from four overlapping promoters and that the rot regulatory region is unusually compact, containing a close array of sites for DNA-binding proteins. The three most upstream rot promoters are activated by the global gene regulatory cAMP-CRP complex and negatively regulated by the CytR repressor protein. Activation of these three promoters occurs by binding of cAMP-CRP to two sites separated by 53 bp. Moreover, one of the cAMP-CRP complexes is involved in the activation of both a Class I and a Class II promoter. Repression takes place by the formation of a CytR/cAMP-CRP/DNA nucleoprotein complex consisting of the two cAMP-CRP molecules and CytR bound in between. The two regulators bind co-operatively to the DNA overlapping the three upstream promoters, simultaneously quenching the cAMP-CRP activator function. These results expand the CytR regulon to include a gene whose product has no known function in ribo- and deoxyribonucleoside catabolism or transport.