Part:BBa_K2996703
RpoA, DNA-directed RNA polymerase subunit alpha
RpoA encodes the DNA-directed RNA polymerase subunit alpha, which plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. It may activate transcription more effectively, compared to RpoZ used in other experiments.
This RpoA-dCas9 fusion protein should be an innovated transcription activator.
Background
DNA-directed RNA polymerases are responsible for the polymerization of ribonucleotides into a sequence complementary to the template DNA. Most RNA polymerases are multimeric enzymes and are composed of a variable number of subunits. The core RNA polymerase complex consists of five subunits (two alpha, one beta, one beta-prime and one omega) and is sufficient for transcription elongation and termination but is unable to initiate transcription. Transcription initiation from promoter elements requires a sixth, dissociable subunit called a sigma factor, which reversibly associates with the core RNA polymerase complex to form a holoenzyme. The core RNA polymerase complex forms a "crab claw"-like structure with an internal channel running along the full length. The key functional sites of the enzyme, as defined by mutational and cross-linking analysis, are located on the inner wall of this channel.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 459
- 1000COMPATIBLE WITH RFC[1000]
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