A peptide from Tetrahymena disrupts subunit organization of E. coli RNA polymerase.
Incubation of the E. coli RNA polymerase with a polypeptide factor from the protozoan Tetrahymena reduces the affinity of the holoenzyme for DNA. SDS-polyacrylamide gel electrophoresis of the peptide-treated RNA polymerase showed that the band pattern of the polymerase subunits was strongly altered. The three large subunits, beta', beta and sigma, disappear and a high number of rapidly migrating bands appeared. However, a brief heat treatment of the samples almost restored the original RNA polymerase subunit composition, and in addition a high molecular weight protein band approximately 240 kDa appeared. It is suggested that the Tetrahymena peptide specifically binds to the RNA polymerase and changes the structures of the large subunits.
Andersen
H A
HA
Department of Biochemistry B, Panum Institute, University of Copenhagen, Denmark.
D000818:Animals; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000187:drug effects*; D004926:Escherichia coli / Q000201:enzymology; D008970:Molecular Weight; D010455:Peptides / Q000302:isolation & purification / Q000494:pharmacology*; D011487:Protein Conformation / Q000187:drug effects; D013769:Tetrahymena pyriformis / Q000378:metabolism*
D010455:Peptides; D012321:DNA-Directed RNA Polymerases