Abstract
One step in the regulation of gene expression that can be controlled by a variety of mechanisms is the transcription of messenger RNA from the DNA template. It is becoming increasingly apparent that an important aspect of such regulation involves transcription termination and its control. Termination sites at the ends of genes or operons provide a signal for RNA polymerase to cease transcribing, thus defining the 3’ end of the primary transcript. Termination signals that reside at other positions in the transcript can also regulate gene expression through the effects of attenuation, retroregulation, and polarity [for reviews see 1,2]. One class of transcription termination events utilized by Escherichia coli and various bacteriophages is dependent upon the action of a protein factor called rho, which participates in the recognition of and response to certain termination sites. Though little is understood about the RNA sequence or structural elements required for rho recognition, a great deal has been learned recently about the structure of rho protein itself. This review will focus on the molecular architecture of rho protein with an emphasis on its domain structure, the interaction of each domain with its substrate, and the interactions between domains that are required for catalysis of transcription termination.
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Dombroski, A.J., Platt, T. (1989). Structure and Function of Rho Factor and Its Role in Transcription Termination. In: Adolph, K.W. (eds) Molecular Biology of Chromosome Function. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3652-8_10
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DOI: https://doi.org/10.1007/978-1-4612-3652-8_10
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