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Literature summary for 2.7.7.6 extracted from

  • Abe, Y.; Fujisaki, N.; Miyoshi, T.; Watanabe, N.; Katayama, T.; Ueda, T.
    Functional analysis of CedA based on its structure: residues important in binding of DNA and RNA polymerase and in the cell division regulation (2016), J. Biochem., 159, 217-223.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A8T7 AND P0A8V2 AND P0A7Z4 DNA-directed RNA polymerase subunits beta, beta', and alpha encoded by genes rpoC, rpoB, and rpoA; genes rpoC, rpoB, and rpoA
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the subunits interact with recombinant His6-tagged CedA, a multi-copy suppressor which represses the dnaAcos inhibition of cell division. Determination of the binding site of CedA for RNA polymerase. The N-terminus of CedA is necessary for a tight interaction Escherichia coli ?
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General Information

General Information Comment Organism
physiological function the enzyme subunits interact with CedA, a multi-copy suppressor which represses the dnaAcos inhibition of cell division. DnaAcos is a mutant of the initiator DnaA that causes overinitiation of chromosome replication in Escherichia coli resulting in inhibition of cell division. Determination of the binding site of CedA for RNA polymerase and examination of the binding functions involved in cell division reactivation Escherichia coli