|PROSITE documentation PDOC00651 [for PROSITE entry PS00830]|
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.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Borukhov S. Sagitov V. Goldfarb A.|
|Title||Transcript cleavage factors from E. coli.|
|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.|