Angiolillo A, Desgro A, Marsili V, Panara F, Gianfranceschi G L
Istituto di Biologia Cellulare, Università di Perugia, Italy.
Experientia. 1993 Oct 15;49(10):902-5. doi: 10.1007/BF01952606.
The effect of the synthetic octapeptide pyroGLU-ASP-ASP-SER-ASP-GLU-GLU-ASN (phosphorylated by casein kinase II, CKII) on DNA transcription by RNA polymerase II has been studied. The peptide contains the acidic carboxy-terminus heptapeptide of the largest subunit of RNA polymerase II, which has been demonstrated to be a phosphorylation site for CKII. The aim of this work is to obtain some insights about the possible role of this domain in RNA polymerase II activity and DNA binding. Results demonstrated that the phosphorylated octapeptide causes strong inhibition of transcription of calf thymus DNA or pSVL SV40 plasmid DNA by RNA polymerase II, when used at concentrations between 0.4-4 micrograms/ml.