PMID:15890417
| Citation |
Richardson, LV and Richardson, JP (2005) Identification of a structural element that is essential for two functions of transcription factor NusG. Biochim. Biophys. Acta 1729:135-40 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1016/j.bbaexp.2005.04.002 |
| Keywords |
DNA-Directed RNA Polymerases/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/physiology; Gene Deletion; Peptide Elongation Factors/chemistry; Peptide Elongation Factors/genetics; Peptide Elongation Factors/physiology; Protein Structure, Tertiary; RNA, Bacterial/metabolism; Rho Factor/metabolism; Transcription Factors/chemistry; Transcription Factors/genetics; Transcription Factors/physiology; Transcription, Genetic; Transcriptional Elongation Factors/physiology |
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