Peptide Analysis of RNA Polymerase Alpha Subunit from Escherichia Coli: Comparison of Free with Assembled Form

Overview

Journal Mol Gen Genet

Specialties Genetics
Molecular Biology

Date 1976 Jun 15

PMID 781518

Citations 2

Authors

M Taketo

A Ishihama

Affiliations

Soon will be listed here.

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.

Citing Articles

Autogenous and post-transcriptional regulation of RNA polymerase synthesis.

Ishihama A, Fukuda R Mol Cell Biochem. 1980; 31(3):177-96.

PMID: 7003354 DOI: 10.1007/BF00225850.

Comparative studies of RNA polymerase subunits from various bacteria.

Fukuda R, Ishihama A, Saitoh T, Taketo M Mol Gen Genet. 1977; 154(2):135-44.

PMID: 408600 DOI: 10.1007/BF00330829.

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