Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10799366 | Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression | 2005 | 6 Pages |
Abstract
The transcription factor NusG from Escherichia coli modulates the rate of transcript elongation by RNA polymerase and the efficiency of Rho-dependent transcript termination. It consists of two globular domains with an extra loop extending out of the amino-terminal domain in the position that is occupied by a third globular domain in some NusG homologues. We have tested the role of this appended mini-domain by assaying the elongation and termination enhancement activities of variants. The results show that variants with changes in their sequence do not cause a loss of functions, whereas variants with the deletions of the residues in that domain are much less active for both functions. This finding suggests that the mini-domain serves as a structural element for an interaction rather than as a site for residue-specific contacts.
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Authors
Lislott V. Richardson, John P. Richardson,