Peptide analysis of RNA polymerase alpha subunit from Escherichia coli: comparison of free with assembled form.

Authors

M Taketo
A Ishihama

Document Type

Article

Publication Date

1976

Keywords

Escherichia-Coli: en, Peptide-Fragments: an, RNA-Polymerases: an

First Page

311

Last Page

316

JAX Source

Mol-Gen-Genet. 1976 Jun 15; 145(3):311-6.

Abstract

The analysis of tryptic peptides was performed on the unassembled as well as assembled form f alpha subunit of the DNA-dependent RNA polymerase from Escherichia coli. The peptide profiles obtained by Dowex 50 column chromatography of the unassembled alpha subunit prepared from cells, either pulse-labeled or continuously labeled with radioactive lysine or arginine, were essentially identical with those of the alpha subunit from intact RNA polymerase. The results suggest that newly synthesized free alpha subunit is assembled into the polymerase structure without any remarkable modifications. The number of lysine- and arginine-containing peaks were close to the values expected from the amino acid composition of alpha subunit assuming that the two alpha subunits in RNA polymerase core enzyme have identical primary structure.

Recommended Citation

Taketo M, Ishihama A. Peptide analysis of RNA polymerase alpha subunit from Escherichia coli: comparison of free with assembled form. Mol-Gen-Genet. 1976 Jun 15; 145(3):311-6.