PROSITE documentation PDOC00651Prokaryotic transcription elongation factors signatures
Bacterial proteins greA and greB [1,2] are necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. Arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked DNA/RNA/ polymerase ternary complexes. Cleavage of the nascent transcript by cleavage factors, such as greA or greB, allows the resumption of elongation from the new 3'terminus. GreA induces cleavage 2 or 3 nucleotides behind the terminus while greB releases longer sequences up to 9 nucleotides in length.
GreA and greB are related proteins of about 160 amino-acid residues. We have developed two signature patterns for this protein family. The first corresponds to a conserved region in the N-terminal section, the second to a region in the C-terminal section.
Last update:December 2004 / Pattern and text revised.
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| 1 | Authors | Borukhov S. Sagitov V. Goldfarb A. |
| Title | Transcript cleavage factors from E. coli. | |
| Source | Cell 72:459-466(1993). | |
| PubMed ID | 8431948 |
| 2 | Authors | Stebbins C.E. Borukhov S. Orlova M. Polyakov A. Goldfarb A. Darst S.A. |
| Title | Crystal structure of the GreA transcript cleavage factor from Escherichia coli. | |
| Source | Nature 373:636-640(1995). | |
| PubMed ID | 7854424 | |
| DOI | 10.1038/373636a0 |
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