Distinct functions of N and C-terminal domains of GreA, an Escherichia coli transcript cleavage factor
- 20 February 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 276 (2) , 379-389
- https://doi.org/10.1006/jmbi.1997.1545
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Transcriptional arrest: Escherichia coli RNA polymerase translocates backward, leaving the 3′ end of the RNA intact and extrudedProceedings of the National Academy of Sciences, 1997
- Domain Organization of Escherichia coli Transcript Cleavage Factors GreA and GreBJournal of Biological Chemistry, 1997
- Promoter Proximal Sequences Modulate RNA Polymerase II Elongation by a Novel MechanismCell, 1996
- Alanine-Scanning Mutagenesis of Human Transcript Elongation Factor TFIISBiochemistry, 1995
- Crystal structure of the GreA transcript cleavage factor from Escherichia coliNature, 1995
- Multiple RNA Polymerase Conformations and GreA: Control of the Fidelity of TranscriptionScience, 1993
- Transcript cleavage factors from E. coliCell, 1993
- Stimulation of transcript elongation requires both the zinc finger and RNA polymerase II binding domains of human TFIISBiochemistry, 1991
- Mapping and characterization of transcriptional pause sites in the early genetic region of bacteriophage T7Journal of Molecular Biology, 1987
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976