Domain organization of RNA polymerase α subunit: C-terminal 85 amino acids constitute a domain capable of dimerization and DNA binding
- 1 September 1994
- Vol. 78 (5), 889-896
- https://doi.org/10.1016/s0092-8674(94)90682-3
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Characterization of the activating region of Escherichia coli catabolite gene activator protein (CAP) II. Role at class I and class II CAP-dependent promotersJournal of Molecular Biology, 1994
- Factor Independent Activation of rrnB P1Journal of Molecular Biology, 1994
- Prediction of Protein Secondary Structure at Better than 70% AccuracyJournal of Molecular Biology, 1993
- Role of the RNA polymerase α subunit in transcription activationMolecular Microbiology, 1992
- Mapping the cAMP receptor protein contact site on the α subunit of Escherichia coli RNA polymeraseMolecular Microbiology, 1992
- Functional specialization within the α-subunit of Escherichia coli RNA polymeraseJournal of Molecular Biology, 1991
- Factor-independent activation of Escherichia coli rRNA transcriptionJournal of Molecular Biology, 1991
- Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroismJournal of Molecular Biology, 1980
- Action of stapeylococcal proteinase on peptides of varying chain length and compositionBiochemical and Biophysical Research Communications, 1976
- Structural Studies of ImmunoglobulinsScience, 1973