Open AccessTHE INTERACTION OF RNA POLYMERASE WITH HISTONES
Author(s) -
Thomas C. Spelsberg,
Sharon Tankersley,
Lubomir S. Hnilica
Publication year - 1969
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.62.4.1218
Subject(s) - polymerase , histone , rna polymerase , rna , histone modifying enzymes , biology , microbiology and biotechnology , small nuclear rna , dna , rna polymerase ii , rna dependent rna polymerase , biochemistry , chemistry , histone h2a , gene expression , gene , promoter
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.
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