THE INTERACTION OF RNA POLYMERASE WITH HISTONES*

  1. Thomas C. Spelsberg,
  2. Sharon Tankersley, and
  3. Lubomir S. Hnilica
  1. DEPARTMENT OF BIOCHEMISTRY, THE UNIVERSITY OF TEXAS M. D. ANDERSON HOSPITAL AND TUMOR INSTITUTE, HOUSTON

Abstract

Arginine-rich histones (F3) interact with both the bacterial and mammalian RNA polymerase and inhibit the in vitro RNA synthesis to a much greater extent than when associated with the DNA template. The lysine-rich histones (F1) inhibit the RNA synthesis mainly through template inhibition. Neither histone fraction displayed such an interaction with DNA polymerase. The RNA polymerase-F3 histone interaction takes place at ionic strength equal to or greater than those occurring in living cells, suggesting a possible role of arginine-rich histones in the regulation of RNA synthesis.

Footnotes

  • ↵ * Supported by U.S. Public Health Service grant CA-07746, American Cancer Society grants E-388 and IN-43-I-1, and The Robert A. Welch Foundation grant G-138.

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  1. PNAS 1969-04 vol. 62 no. 4 1218-1225
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